PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 24012499-8 2013 Treatment with cycloheximide indicated that increased m-SR was due to de novo protein synthesis associated with phospho-active forms of ERK1/2, MARCKS, Akt and rapamycin-sensitive mTOR. Cycloheximide 15-28 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 24022404-0 2014 Myristoylated alanine-rich C kinase substrate coordinates native TRPC1 channel activation by phosphatidylinositol 4,5-bisphosphate and protein kinase C in vascular smooth muscle. Phosphatidylinositol 4,5-Diphosphate 93-130 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 24022404-3 2014 The present study reveals that myristoylated alanine-rich C kinase substrate (MARCKS) protein coordinates activation of TRPC1 channels by PKC and PI(4,5)P2. pi(4,5)p2 146-155 myristoylated alanine rich protein kinase C substrate Homo sapiens 31-76 24022404-3 2014 The present study reveals that myristoylated alanine-rich C kinase substrate (MARCKS) protein coordinates activation of TRPC1 channels by PKC and PI(4,5)P2. pi(4,5)p2 146-155 myristoylated alanine rich protein kinase C substrate Homo sapiens 78-84 24022404-4 2014 TRPC1 channels and MARCKS form signaling complexes with PI(4,5)P2 bound to MARCKS; in this configuration TRPC1 channels are closed. pi(4,5)p2 56-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 24022404-4 2014 TRPC1 channels and MARCKS form signaling complexes with PI(4,5)P2 bound to MARCKS; in this configuration TRPC1 channels are closed. pi(4,5)p2 56-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-81 24022404-5 2014 Activators of TRPC1 channels induce PKC phosphorylation of TRPC1 proteins, which causes dissociation of TRPC1 subunits from MARCKS and release of PI(4,5)P2 from MARCKS; PI(4,5)P2 subsequently binds to TRPC1 subunits to induce channel opening. pi(4,5)p2 146-155 myristoylated alanine rich protein kinase C substrate Homo sapiens 161-167 24022404-6 2014 Calmodulin acting at, or upstream of, MARCKS is also required for TRPC1 channel opening through a similar gating mechanism involving PKC and PI(4,5)P2. pi(4,5)p2 141-150 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-44 24022404-7 2014 These novel findings show that MARCKS coordinates native TRPC1 channel activation in VSMCs by acting as a reversible PI(4,5)P2 buffer, which is regulated by PKC-mediated TRPC1 phosphorylation. pi(4,5)p2 buffer 117-133 myristoylated alanine rich protein kinase C substrate Homo sapiens 31-37 24085052-8 2013 Downstream signaling was investigated by measuring the amount of phosphorylated Myristoylated Alanine-rich C-kinase substrate (MARCKS) and extracellular signal-regulated kinases (ERK) 1/2 of valrubicin-stimulated keratinocytes. valrubicin 191-201 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 23876235-6 2013 Phosphorylation of the tyrosine kinase Yes and expression of the actin-binding protein myristoylated alanine-rich C-kinase substrate (MARCKS) were increased two- and eightfold in TamR cells respectively, and these proteins were selected for further analysis. Alanine 101-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23876235-10 2013 These findings provide network-level insights into the molecular alterations associated with the tamoxifen-resistant phenotype, and identify MARCKS as a potential biomarker of therapeutic responsiveness that may assist in stratification of patients for optimal therapy. Tamoxifen 97-106 myristoylated alanine rich protein kinase C substrate Homo sapiens 141-147 23970349-3 2013 In this study, we aimed to isolate and characterize a small population of CD133+ cells that existed in the HCC cell line SMMC-7721 by MACS and investigated the possible roles of 8-bromo-7-methoxychrysin (BrMC), a synthetic analogue of chrysin, in inhibiting the properties of CD133+ sphere-forming cells (SFCs) derived from the HCC cell line SMMC-7721, namely liver cancer stem cells (LCSCs). smmc 121-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-138 23377348-8 2013 MARCKS translocated rapidly from plasma membrane to cytoplasm, whereas HSP70 was observed in the cytoplasm and appeared to associate with MARCKS after PMA exposure. Tetradecanoylphorbol Acetate 151-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-144 24040334-13 2013 pluriSelect separation was substantially faster than MACS (1h vs. 2.5h) and no pre-enrichment steps were necessary. Hydrogen 59-61 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-57 23424156-0 2013 Taurolithocholate-induced MRP2 retrieval involves MARCKS phosphorylation by protein kinase Cepsilon in HUH-NTCP Cells. Taurolithocholic Acid 0-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 50-56 23424156-11 2013 TLC and phorbol myristate acetate increased cytosolic pMARCKS and decreased PM-MARCKS in HuH-NTCP cells. Tetradecanoylphorbol Acetate 8-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 55-61 23704996-0 2013 MARCKS protein is phosphorylated and regulates calcium mobilization during human acrosomal exocytosis. Calcium 47-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 23704996-4 2013 Calcium- and phorbol ester-triggered acrosomal exocytosis in permeabilized sperm was abrogated by different anti-MARCKS antibodies raised against two different domains, indicating that the protein participates in acrosomal exocytosis. Calcium 0-7 myristoylated alanine rich protein kinase C substrate Homo sapiens 113-119 23704996-4 2013 Calcium- and phorbol ester-triggered acrosomal exocytosis in permeabilized sperm was abrogated by different anti-MARCKS antibodies raised against two different domains, indicating that the protein participates in acrosomal exocytosis. Phorbol Esters 13-26 myristoylated alanine rich protein kinase C substrate Homo sapiens 113-119 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Phosphatidylinositol 4,5-Diphosphate 14-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 76-82 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Phosphatidylinositol 4,5-Diphosphate 14-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Phosphatidylinositol 4,5-Diphosphate 14-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A 23-35 myristoylated alanine rich protein kinase C substrate Homo sapiens 76-82 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A 23-35 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. adenophostin A 23-35 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Phosphatidylinositol 4,5-Diphosphate 187-191 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Phosphatidylinositol 4,5-Diphosphate 187-191 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Calcium 244-251 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-9 2013 We found that PIP2 and adenophostin, a potent IP3-receptor agonist, rescued MARCKS inhibition in permeabilized sperm, suggesting that MARCKS inhibits acrosomal exocytosis by sequestering PIP2 and, indirectly, MARCKS regulates the intracellular calcium mobilization. Calcium 244-251 myristoylated alanine rich protein kinase C substrate Homo sapiens 134-140 23704996-10 2013 In non-permeabilized sperm, a permeable peptide of MARCKS ED also inhibited acrosomal exocytosis when stimulated by a natural agonist such as progesterone, and pharmacological inducers such as calcium ionophore and phorbol ester. Progesterone 142-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 23704996-10 2013 In non-permeabilized sperm, a permeable peptide of MARCKS ED also inhibited acrosomal exocytosis when stimulated by a natural agonist such as progesterone, and pharmacological inducers such as calcium ionophore and phorbol ester. Calcium 193-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 23704996-10 2013 In non-permeabilized sperm, a permeable peptide of MARCKS ED also inhibited acrosomal exocytosis when stimulated by a natural agonist such as progesterone, and pharmacological inducers such as calcium ionophore and phorbol ester. Phorbol Esters 215-228 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Calcium 88-95 myristoylated alanine rich protein kinase C substrate Homo sapiens 52-58 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Calcium 88-95 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Progesterone 113-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 52-58 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Progesterone 113-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Calcium 163-170 myristoylated alanine rich protein kinase C substrate Homo sapiens 52-58 23704996-11 2013 The preincubation of human sperm with the permeable MARCKS ED abolished the increase in calcium levels caused by progesterone, demonstrating that MARCKS regulates calcium mobilization. Calcium 163-170 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 23704996-13 2013 Altogether, these results show that MARCKS is a negative modulator of the acrosomal exocytosis, probably by sequestering PIP2, and that it is phosphorylated during acrosomal exocytosis. Phosphatidylinositol 4,5-Diphosphate 121-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 23377348-4 2013 The results indicate that HSP70 interaction with MARCKS is enhanced after exposure of the cells to the protein kinase C activator/mucin secretagogue, phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 150-181 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 23377348-4 2013 The results indicate that HSP70 interaction with MARCKS is enhanced after exposure of the cells to the protein kinase C activator/mucin secretagogue, phorbol 12-myristate 13-acetate (PMA). Tetradecanoylphorbol Acetate 183-186 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 23377348-5 2013 Pretreatment of NHBEs with MAL3-101 attenuated in a concentration-dependent manner PMA-stimulated mucin secretion and interactions among HSP70, MARCKS, and CSP. mal3-101 27-35 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 23377348-5 2013 Pretreatment of NHBEs with MAL3-101 attenuated in a concentration-dependent manner PMA-stimulated mucin secretion and interactions among HSP70, MARCKS, and CSP. Tetradecanoylphorbol Acetate 83-86 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 23476444-1 2013 The title compound, C22H21Cl2NO, is a derivative of mono-carbonyl analogues of curcumin (MACs). c22h21cl2no 20-31 myristoylated alanine rich protein kinase C substrate Homo sapiens 89-93 23075500-6 2013 We have successfully identified a 25-mer peptide, MARCKS-ED, based on the effector domain sequence of the intracellular membrane protein myristoylated alanine-rich C-kinase substrate that can recognize PS with preferences for highly curved vesicles in a sequence-specific manner. Phosphorus 202-204 myristoylated alanine rich protein kinase C substrate Homo sapiens 50-56 23476444-1 2013 The title compound, C22H21Cl2NO, is a derivative of mono-carbonyl analogues of curcumin (MACs). Curcumin 79-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 89-93 23116317-0 2013 Promising curcumin-based drug design: mono-carbonyl analogues of curcumin (MACs). Curcumin 10-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-79 23116317-0 2013 Promising curcumin-based drug design: mono-carbonyl analogues of curcumin (MACs). Curcumin 65-73 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-79 23116317-7 2013 Particularly, the latter called mono-carbonyl analogs of curcumin (MACs) has been reported to has an enhanced stability in vitro and an improved pharmacokinetic profile in vivo. Curcumin 57-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 67-71 23116317-8 2013 Thus, MACs have attracted a high attention for development of new curcumin-based agents with both enhanced bioactivities and pharmacokinetic profiles. Curcumin 66-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 6-10 22013076-0 2011 Sequestration of phosphoinositides by mutated MARCKS effector domain inhibits stimulated Ca(2+) mobilization and degranulation in mast cells. Phosphatidylinositols 17-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 46-52 22667591-7 2012 Our model properly describes the saturation of lipids on membrane surfaces, and correctly predicts that the MARCKS peptide can consistently sequester three multivalent phosphatidylinositol 4,5-bisphosphate lipids through its basic amino acid residues, regardless of a wide range of the percentage of monovalent phosphatidylserine in the membrane. phosphatidylinositol 4,5-bisphosphate lipids 168-212 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 22667591-7 2012 Our model properly describes the saturation of lipids on membrane surfaces, and correctly predicts that the MARCKS peptide can consistently sequester three multivalent phosphatidylinositol 4,5-bisphosphate lipids through its basic amino acid residues, regardless of a wide range of the percentage of monovalent phosphatidylserine in the membrane. Amino Acids, Basic 225-241 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 22667591-7 2012 Our model properly describes the saturation of lipids on membrane surfaces, and correctly predicts that the MARCKS peptide can consistently sequester three multivalent phosphatidylinositol 4,5-bisphosphate lipids through its basic amino acid residues, regardless of a wide range of the percentage of monovalent phosphatidylserine in the membrane. Phosphatidylserines 311-329 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 22568990-4 2012 We also identified myristoylated alanine-rich C-kinase substrate (MARCKS), heat shock proteins and actin as L-PGDS-binding proteins, demonstrating that MARCKS/Akt/Rho/Jnk pathways are involved in the L-PGDS actions in glia. Alanine 33-40 myristoylated alanine rich protein kinase C substrate Homo sapiens 152-158 22773836-0 2012 Angiotensin-II and MARCKS: a hydrogen peroxide- and RAC1-dependent signaling pathway in vascular endothelium. Hydrogen Peroxide 29-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 22773836-6 2012 In endothelial cells, angiotensin-II-promoted MARCKS phosphorylation is abrogated by PEG-catalase, implicating endogenous H(2)O(2) in the angiotensin-II response. Hydrogen Peroxide 122-130 myristoylated alanine rich protein kinase C substrate Homo sapiens 46-52 22773836-10 2012 Cell imaging studies using a phosphoinositide 4,5-bisphosphate (PIP(2)) biosensor revealed that angiotensin-II PIP(2) regulation depends on MARCKS and H(2)O(2). phosphoinositide 4,5-bisphosphate 29-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-146 22773836-12 2012 These studies establish a critical role for H(2)O(2) in angiotensin-II signaling to the endothelial cytoskeleton in a novel pathway that is critically dependent on MARCKS, Rac1, and c-Abl. Hydrogen Peroxide 44-52 myristoylated alanine rich protein kinase C substrate Homo sapiens 164-170 21763456-4 2012 MARCKS protein expression was found prominently in inflammatory cells of Opisthorchis viverrini-treated as well as O. viverrini plus N-nitrosodimethylamine (NDMA)-treated hamsters from week 2 to week 3 of treatment. Dimethylnitrosamine 133-155 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 21763456-4 2012 MARCKS protein expression was found prominently in inflammatory cells of Opisthorchis viverrini-treated as well as O. viverrini plus N-nitrosodimethylamine (NDMA)-treated hamsters from week 2 to week 3 of treatment. Dimethylnitrosamine 157-161 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 21448919-4 2012 By contrast, PKC activation by the phorbol ester phorbol 12,13-dibutyrate (PDBu) elicited MARCKS phosphorylation which lasted more than 10 min. Phorbol Esters 35-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 21448919-4 2012 By contrast, PKC activation by the phorbol ester phorbol 12,13-dibutyrate (PDBu) elicited MARCKS phosphorylation which lasted more than 10 min. Phorbol 12,13-Dibutyrate 49-73 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 21448919-4 2012 By contrast, PKC activation by the phorbol ester phorbol 12,13-dibutyrate (PDBu) elicited MARCKS phosphorylation which lasted more than 10 min. Phorbol 12,13-Dibutyrate 75-79 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 21448919-6 2012 Protein phosphatase (PP) 2A inhibitors calyculin A and fostriecin inhibited the dephosphorylation of MARCKS after BK-induced phosphorylation. fostriecin 55-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 101-107 22013076-2 2011 We investigated the hypothesis that the polybasic effector domain (ED) of the abundant intracellular substrate for protein kinase C known as myristoylated alanine-rich protein kinase C substrate (MARCKS) sequesters phosphoinositides at the inner leaflet of the plasma membrane until MARCKS dissociates after phosphorylation by activated PKC. Phosphatidylinositols 215-232 myristoylated alanine rich protein kinase C substrate Homo sapiens 196-202 22013076-2 2011 We investigated the hypothesis that the polybasic effector domain (ED) of the abundant intracellular substrate for protein kinase C known as myristoylated alanine-rich protein kinase C substrate (MARCKS) sequesters phosphoinositides at the inner leaflet of the plasma membrane until MARCKS dissociates after phosphorylation by activated PKC. Phosphatidylinositols 215-232 myristoylated alanine rich protein kinase C substrate Homo sapiens 283-289 22013076-5 2011 We find that MARCKS-ED dissociation is prevented by mutation of four serine residues that are potential sites of phosphorylation by PKC. Serine 69-75 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 22013076-2 2011 We investigated the hypothesis that the polybasic effector domain (ED) of the abundant intracellular substrate for protein kinase C known as myristoylated alanine-rich protein kinase C substrate (MARCKS) sequesters phosphoinositides at the inner leaflet of the plasma membrane until MARCKS dissociates after phosphorylation by activated PKC. Phosphatidylinositols 215-232 myristoylated alanine rich protein kinase C substrate Homo sapiens 141-194 21762971-9 2011 Four serine residues in the myristoylated alanine-rich C kinase substrate (MARCKS)-phosphorylation site domain were mutated to identify the function of MARCKS in TRPM8-mediated airway mucus hypersecretion. Serine 5-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-73 22013076-6 2011 Cells expressing this mutated MARCKS-ED SA4 show delayed onset of antigen-stimulated Ca(2+) mobilization and substantial inhibition of granule exocytosis. sa4 40-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-36 22013076-7 2011 Stimulation of degranulation by thapsigargin, which bypasses inositol 1,4,5-trisphosphate production, is also substantially reduced in the presence of MARCKS-ED SA4, but store-operated Ca(2+) entry is not inhibited. Thapsigargin 32-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 22013076-7 2011 Stimulation of degranulation by thapsigargin, which bypasses inositol 1,4,5-trisphosphate production, is also substantially reduced in the presence of MARCKS-ED SA4, but store-operated Ca(2+) entry is not inhibited. Inositol 1,4,5-Trisphosphate 61-89 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 22013076-8 2011 These results show the capacity of MARCKS-ED to regulate granule exocytosis in a PKC-dependent manner, consistent with regulated sequestration of phosphoinositides that mediate granule fusion at the plasma membrane. Phosphatidylinositols 146-163 myristoylated alanine rich protein kinase C substrate Homo sapiens 35-41 21762971-9 2011 Four serine residues in the myristoylated alanine-rich C kinase substrate (MARCKS)-phosphorylation site domain were mutated to identify the function of MARCKS in TRPM8-mediated airway mucus hypersecretion. Serine 5-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-81 20651816-7 2010 Thus, the present review proposes that MARCKS may be implicated in Abeta generation, by modulating free PIP2 level and actin movement, causing endocytosis. Phosphatidylinositol 4,5-Diphosphate 104-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 39-45 21320438-0 2011 Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C. The binding of the MARCKS peptide to the lipid monolayer containing PIP(2) increases the lateral pressure of the monolayer. Phosphatidylinositol 4,5-Diphosphate 218-224 myristoylated alanine rich protein kinase C substrate Homo sapiens 121-127 21320438-0 2011 Oscillations in the lateral pressure of lipid monolayers induced by nonlinear chemical dynamics of the second messengers MARCKS and protein kinase C. The binding of the MARCKS peptide to the lipid monolayer containing PIP(2) increases the lateral pressure of the monolayer. Phosphatidylinositol 4,5-Diphosphate 218-224 myristoylated alanine rich protein kinase C substrate Homo sapiens 169-175 21072051-5 2011 Also, reduced phosphorylation of the actin filament crosslinking protein myristoylated alanine-rich C-kinase substrate (MARCKS) in response to suppression of p22(phox) hints at a novel effector of NOX signaling. nicotine 1-N-oxide 197-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 21097841-0 2011 The MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cells. Phosphatidylinositol 4,5-Diphosphate 44-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-10 20559679-6 2010 In addition, PI(4,5)P(2) can accumulate at sphingolipid/cholesterol-based rafts following activation of distinct membrane receptors or be sequestered in a reversible manner due to electrostatic constrains posed by proteins like MARCKS. pi(4,5)p(2) 13-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 228-234 20047593-6 2010 Using a confocal microscopic analysis of CCA cell lines that had been stimulated with the PKC activator, 12-0-tetradecanoyl phorbol-13-acetate (TPA), MARCKS was found to be translocated from the plasma membrane to the perinuclear area. 12-0-tetradecanoyl phorbol-13-acetate 105-142 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 20047593-6 2010 Using a confocal microscopic analysis of CCA cell lines that had been stimulated with the PKC activator, 12-0-tetradecanoyl phorbol-13-acetate (TPA), MARCKS was found to be translocated from the plasma membrane to the perinuclear area. Tetradecanoylphorbol Acetate 144-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 20047593-9 2010 Interestingly, after TPA stimulation, the CCA cell line-depleted MARCKS showed a decrease in migration and invasion activity. Tetradecanoylphorbol Acetate 21-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 20047593-11 2010 After TPA stimulation, PKC phosphorylates MARCKS leading to cell migration or invasion. Tetradecanoylphorbol Acetate 6-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 42-48 19362071-0 2009 Interaction of the MARCKS peptide with PIP2 in phospholipid monolayers. Phosphatidylinositol 4,5-Diphosphate 39-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 19852062-9 2010 In line with cMSI induced functional inactivation of MARCKS, 8 out of 11 MSI-H adenocarcinomas showed regional or complete loss of the protein. cmsi 13-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 19602578-9 2009 hIDS overexpression induced phosphorylation of protein kinase C (PKC) alpha and its newly myristoylated alanine-rich C kinase substrate, MARCKS. HIDS 0-4 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-143 19602578-10 2009 We conclude that IDS has a role in glucose-stimulated insulin secretion via a mechanism that involves the activation of exocytosis through phosphorylation of PKCalpha and MARCKS. Glucose 35-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 171-177 19885570-7 2009 The combination of safingol/irinotecan at 1:1 molar ratio was found to be additive in HT-29 cells (CI=0.94) and synergistic in LS-174T cells (CI=0.68), and resulted in concentration- and time-dependent down-regulation of p-PKC and p-MARCKS. safingol 19-27 myristoylated alanine rich protein kinase C substrate Homo sapiens 233-239 19885570-7 2009 The combination of safingol/irinotecan at 1:1 molar ratio was found to be additive in HT-29 cells (CI=0.94) and synergistic in LS-174T cells (CI=0.68), and resulted in concentration- and time-dependent down-regulation of p-PKC and p-MARCKS. Irinotecan 28-38 myristoylated alanine rich protein kinase C substrate Homo sapiens 233-239 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. Ro 31-8220 32-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 143-149 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. Ro 31-8220 32-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. fasudil 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 143-149 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. fasudil 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. Y 27632 82-88 myristoylated alanine rich protein kinase C substrate Homo sapiens 143-149 19475567-4 2009 The protein kinase C inhibitor, Ro-31-8220, and Rho-kinase inhibitors, HA1077 and Y27632, themselves decreased basal phosphorylation levels of MARCKS and coincidently elicited translocation of MARCKS to lipid rafts. Y 27632 82-88 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 19475567-5 2009 On the other hand, the phosphoinositide 3-kinase inhibitor, LY294002, abolished IGF-I-induced dephosphorylation, translocation of MARCKS to lipid rafts, and lamellipodia formation. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 60-68 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 19475567-6 2009 Treatment of cells with neomycin, a PIP2-masking reagent, attenuated the translocation of MARCKS to lipid rafts and the lamellipodia formation induced by IGF-I, although dephosphorylation of MARCKS was not affected. Neomycin 24-32 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 19475567-6 2009 Treatment of cells with neomycin, a PIP2-masking reagent, attenuated the translocation of MARCKS to lipid rafts and the lamellipodia formation induced by IGF-I, although dephosphorylation of MARCKS was not affected. Neomycin 24-32 myristoylated alanine rich protein kinase C substrate Homo sapiens 191-197 19475567-6 2009 Treatment of cells with neomycin, a PIP2-masking reagent, attenuated the translocation of MARCKS to lipid rafts and the lamellipodia formation induced by IGF-I, although dephosphorylation of MARCKS was not affected. Phosphatidylinositol 4,5-Diphosphate 36-40 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 19475567-7 2009 Immunocytochemical and immunoprecipitation analysis indicated that IGF-I stimulation induced the translocation of MARCKS to lipid rafts in the edge of lamellipodia and formation of the complex with PIP2. Phosphatidylinositol 4,5-Diphosphate 198-202 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-120 19475567-9 2009 These results suggest a novel role for MARCKS in lamellipodia formation induced by IGF-I via the translocation of MARCKS, association with PIP2, and accumulation of beta-actin in the membrane microdomains. Phosphatidylinositol 4,5-Diphosphate 139-143 myristoylated alanine rich protein kinase C substrate Homo sapiens 39-45 19362071-0 2009 Interaction of the MARCKS peptide with PIP2 in phospholipid monolayers. Phospholipids 47-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 19362071-1 2009 In this present work we have studied the effect of MARCKS (151-175) peptide on a mixed DPPC/PIP2 monolayer. 1,2-Dipalmitoylphosphatidylcholine 87-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 19362071-1 2009 In this present work we have studied the effect of MARCKS (151-175) peptide on a mixed DPPC/PIP2 monolayer. Phosphatidylinositol 4,5-Diphosphate 92-96 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 19362071-4 2009 This elongation forms the precondition for the electrostatic interaction of the MARCKS peptide with the PIP2 molecules. Phosphatidylinositol 4,5-Diphosphate 104-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 80-86 19457106-6 2009 L-type VGCC has the dominant role in ADP of LDCV exocytosis by regulating Protein Kinase C (PKC)-epsilon translocation and phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS), a target molecule of PKC-epsilon. ldcv 44-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 142-187 19457106-6 2009 L-type VGCC has the dominant role in ADP of LDCV exocytosis by regulating Protein Kinase C (PKC)-epsilon translocation and phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS), a target molecule of PKC-epsilon. ldcv 44-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 189-195 19457106-10 2009 Taken together, we suggest that L-type VGCC in lipid rafts selectively mediates ADP of LDCV exocytosis by regulating PKC-epsilon translocation and MARCKS phosphorylation. ldcv 87-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 147-153 18502797-1 2008 The binding of the myristoylated alanine-rich C kinase substrate (MARCKS) to mixed, fluid, phospholipid membranes is modeled with a recently developed Monte Carlo simulation scheme. Phospholipids 91-103 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-64 18789340-4 2009 Phosphorylation of MARCKS, a marker of PKC activity, was increased in the prefrontal cortex of animals treated with the psychostimulant amphetamine, as well as in sleep-deprived animals (another animal model of mania), but decreased in lithium-treated animals. Amphetamine 136-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 18789340-4 2009 Phosphorylation of MARCKS, a marker of PKC activity, was increased in the prefrontal cortex of animals treated with the psychostimulant amphetamine, as well as in sleep-deprived animals (another animal model of mania), but decreased in lithium-treated animals. Lithium 236-243 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 18789340-5 2009 The antidepressant imipramine, which shows pro-manic properties in patients with bipolar disorder (BPD), also enhanced phospho-MARCKS in prefrontal cortex in vivo. Imipramine 19-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 18768137-5 2008 MARCKS phosphorylation is switched on by treatment with PKC agonist PMA (Phorbol 12-Myristate 13-Acetate). Tetradecanoylphorbol Acetate 68-71 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 18768137-5 2008 MARCKS phosphorylation is switched on by treatment with PKC agonist PMA (Phorbol 12-Myristate 13-Acetate). Tetradecanoylphorbol Acetate 73-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 18768137-6 2008 Consistently, the broad PKC inhibitor BMI (Bisindolyl Maleimide I) abrogates MARCKS phosphorylation. bisindolylmaleimide I 38-41 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 18768137-6 2008 Consistently, the broad PKC inhibitor BMI (Bisindolyl Maleimide I) abrogates MARCKS phosphorylation. bisindolylmaleimide I 43-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 18799624-0 2008 Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching. Alanine 41-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 27-40 18799624-0 2008 Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphatidylinositol-4,5-diphosphate signaling is critical for dendrite branching. Phosphatidylinositol 4,5-Diphosphate 73-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 27-40 18799624-2 2008 Here, we show that increasing the level of myristoylated, alanine-rich C kinase substrate (MARCKS), a prominent substrate of protein kinase C and a phosphatidylinositol-4,5-diphosphate [PI(4,5)P2] sequestration protein highly expressed in the brain, enhanced branching and growth of dendrites both in vitro and in vivo. Phosphatidylinositol 4,5-Diphosphate 148-184 myristoylated alanine rich protein kinase C substrate Homo sapiens 43-89 18799624-2 2008 Here, we show that increasing the level of myristoylated, alanine-rich C kinase substrate (MARCKS), a prominent substrate of protein kinase C and a phosphatidylinositol-4,5-diphosphate [PI(4,5)P2] sequestration protein highly expressed in the brain, enhanced branching and growth of dendrites both in vitro and in vivo. Phosphatidylinositol 4,5-Diphosphate 148-184 myristoylated alanine rich protein kinase C substrate Homo sapiens 91-97 18799624-2 2008 Here, we show that increasing the level of myristoylated, alanine-rich C kinase substrate (MARCKS), a prominent substrate of protein kinase C and a phosphatidylinositol-4,5-diphosphate [PI(4,5)P2] sequestration protein highly expressed in the brain, enhanced branching and growth of dendrites both in vitro and in vivo. pi(4,5)p2 186-195 myristoylated alanine rich protein kinase C substrate Homo sapiens 43-89 18799624-2 2008 Here, we show that increasing the level of myristoylated, alanine-rich C kinase substrate (MARCKS), a prominent substrate of protein kinase C and a phosphatidylinositol-4,5-diphosphate [PI(4,5)P2] sequestration protein highly expressed in the brain, enhanced branching and growth of dendrites both in vitro and in vivo. pi(4,5)p2 186-195 myristoylated alanine rich protein kinase C substrate Homo sapiens 91-97 18799624-7 2008 These findings demonstrate a critical role for MARCKS-PI(4,5)P2 signaling in regulating dendrite development. (4,5)p2 56-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 18852131-7 2008 Using a proteomic profiling analysis with isotope tags for relative and absolute quantitation labeling technique, we have identified 20 down-regulated proteins and 42 up-regulated proteins on IPI-504 treatment.tumor growth Identical changes were observed in the expression of the genes coding for these proteins in a subset of proteins including HSPA1B, LGALS3, CALM1, FAM84B, FDPS, GOLPH2, HBA1, HIST1H1C, HLA-B, and MARCKS. diprotin A 192-195 myristoylated alanine rich protein kinase C substrate Homo sapiens 418-424 19168130-6 2009 Following induction of PKCepsilonA/E-expression by doxycycline for 24 h and additional short-term treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA), PKCepsilonA/E translocated to the plasma membrane and increased phosphorylation of MARCKS(S152/156). Tetradecanoylphorbol Acetate 113-149 myristoylated alanine rich protein kinase C substrate Homo sapiens 240-246 19168130-8 2009 MARCKS was not phosphorylated after treatment with TPA alone, demonstrating that in this system it is phosphorylated only by PKCepsilon localized to the plasma membrane but not by PKCalpha or delta, the other TPA-responsive PKC isozymes in HeLa cells. Tetradecanoylphorbol Acetate 51-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 19168130-8 2009 MARCKS was not phosphorylated after treatment with TPA alone, demonstrating that in this system it is phosphorylated only by PKCepsilon localized to the plasma membrane but not by PKCalpha or delta, the other TPA-responsive PKC isozymes in HeLa cells. Tetradecanoylphorbol Acetate 209-212 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 19133142-11 2009 MACS efficiently eliminates EPS spermatozoa. eps 28-31 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 19133142-12 2009 MACS combined with DGC allows a mean reduction of 70% in EPS and of 60% in MMP-disrupted spermatozoa with a mean increase of 50% in sperm survival at 24 h. CONCLUSION: Human ejaculates contain EPS spermatozoa which can mostly be eliminated by DGC plus MACS resulting in improved sperm long term viability, motility and MMP integrity. eps 57-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 19133142-12 2009 MACS combined with DGC allows a mean reduction of 70% in EPS and of 60% in MMP-disrupted spermatozoa with a mean increase of 50% in sperm survival at 24 h. CONCLUSION: Human ejaculates contain EPS spermatozoa which can mostly be eliminated by DGC plus MACS resulting in improved sperm long term viability, motility and MMP integrity. eps 193-196 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 19133142-12 2009 MACS combined with DGC allows a mean reduction of 70% in EPS and of 60% in MMP-disrupted spermatozoa with a mean increase of 50% in sperm survival at 24 h. CONCLUSION: Human ejaculates contain EPS spermatozoa which can mostly be eliminated by DGC plus MACS resulting in improved sperm long term viability, motility and MMP integrity. eps 193-196 myristoylated alanine rich protein kinase C substrate Homo sapiens 252-256 19165341-9 2009 The localization of the polybasic effector domain of MARCKS illustrates the non-nuclear aspect of the polyphosphoinositides. Phosphatidylinositol Phosphates 102-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 19077250-12 2008 TPA induced phosphorylation of the PKC substrate myristoylated alanine-rich C kinase substrate (MARCKS) which was suppressed by the PKC inhibitors. Tetradecanoylphorbol Acetate 0-3 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 18502797-1 2008 The binding of the myristoylated alanine-rich C kinase substrate (MARCKS) to mixed, fluid, phospholipid membranes is modeled with a recently developed Monte Carlo simulation scheme. Phospholipids 91-103 myristoylated alanine rich protein kinase C substrate Homo sapiens 66-72 18502797-2 2008 The central domain of MARCKS is both basic (zeta = +13) and hydrophobic (five Phe residues), and is flanked with two long chains, one ending with the myristoylated N-terminus. Phenylalanine 78-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 22-28 17996694-2 2007 Using MACS-purified CD4 cells, we found that rapamycin and cyclosporine A (CsA) potently inhibited the TGFbeta and IL-6-induced generation of IL-17-producing cells. Sirolimus 45-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 6-10 18477669-3 2008 In primary human nasal epithelial cells, treatment with TPA led not only to activation of phosphorylation of PKC, myristoylated alanine-rich C kinase substrate, and mitogen-activated protein kinase but also expression of novel PKC-delta, PKC-theta, and PKC-epsilon. Tetradecanoylphorbol Acetate 56-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-159 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Tetradecanoylphorbol Acetate 83-119 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Tetradecanoylphorbol Acetate 83-119 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Ionomycin 123-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Ionomycin 123-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Clopidogrel 141-144 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Clopidogrel 141-144 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Clopidogrel 274-277 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 18296509-7 2008 Microinjecting eggs with mutant-unphosphorylatable MARCKS reduced the intensity of 12-O-tetradecanoylphorbol 13-acetate or ionomycin-induced CGE by 50%, indicating that phosphorylation of MARCKS by novel and/or conventional PKCs (n/cPKCs) is a pivotal event associated with CGE. Clopidogrel 274-277 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 18296509-8 2008 Moreover, we were able to demonstrate cPKCs involvement in ionomycin-induced MARCKS translocation and CGE. Ionomycin 59-68 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 18186025-5 2008 The calculated binding constants of the MARCKS(151-175) peptide and a series of related peptides to mixed PC/PS/PIP2 membranes are in satisfactory agreement with in vitro experiments. pc 106-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 18186025-5 2008 The calculated binding constants of the MARCKS(151-175) peptide and a series of related peptides to mixed PC/PS/PIP2 membranes are in satisfactory agreement with in vitro experiments. Phosphorus 109-111 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 18186025-5 2008 The calculated binding constants of the MARCKS(151-175) peptide and a series of related peptides to mixed PC/PS/PIP2 membranes are in satisfactory agreement with in vitro experiments. Phosphatidylinositol 4,5-Diphosphate 112-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 17825913-3 2008 This transcriptomic profile was compared with that of GMTC prepared by a novel process (CD3-CD28/DeltaNGFR-MACS) that limits alterations. gmtc 54-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-111 17825913-6 2008 Specific analysis of GMTC production processes showed that DeltaNGFR-MACS selection combined with CD3-CD28 activation limits the aberrant expression of genes involved in immunological functions and apoptotic pathways. gmtc 21-25 myristoylated alanine rich protein kinase C substrate Homo sapiens 69-73 17996694-2 2007 Using MACS-purified CD4 cells, we found that rapamycin and cyclosporine A (CsA) potently inhibited the TGFbeta and IL-6-induced generation of IL-17-producing cells. Cyclosporine 59-73 myristoylated alanine rich protein kinase C substrate Homo sapiens 6-10 17996694-2 2007 Using MACS-purified CD4 cells, we found that rapamycin and cyclosporine A (CsA) potently inhibited the TGFbeta and IL-6-induced generation of IL-17-producing cells. Cyclosporine 75-78 myristoylated alanine rich protein kinase C substrate Homo sapiens 6-10 17284528-8 2007 Enzastaurin inhibited Akt phosphorylation and Akt kinase activity, as well as downstream p-MARCKS and ribosomal p-S6. enzastaurin 0-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 91-97 18055557-5 2007 Rottlerin also reduced PMA- or human neutrophil elastase-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells. rottlerin 0-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 84-129 18055557-5 2007 Rottlerin also reduced PMA- or human neutrophil elastase-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) protein in these cells. rottlerin 0-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 131-137 18055557-6 2007 Both secretion and MARCKS phosphorylation were significantly enhanced by the PKC delta activator bryostatin 1. bryostatin 1 97-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 16987960-6 2006 Expression of phosphorylation-deficient, mutant MARCKS greatly expands growth cone adhesion, and this is characterized by extensive colocalization of MARCKS and alpha3-integrin, resistance to eicosanoid-triggered detachment and collapse, and reversal of Sema3A-induced repulsion into attraction. Eicosanoids 192-202 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 17191124-5 2007 Indeed, like other sphingosine-related lipids, ES 285 induces the phosphorylation of MARCKS. Sphingosine 19-30 myristoylated alanine rich protein kinase C substrate Homo sapiens 85-91 17191124-5 2007 Indeed, like other sphingosine-related lipids, ES 285 induces the phosphorylation of MARCKS. Einsteinium 47-49 myristoylated alanine rich protein kinase C substrate Homo sapiens 85-91 17384256-2 2006 Annexin-V-MACS is able to separate apoptotic from nonapoptotic sperm on the basis of their externalization of phosphatidylserine (EPS). Phosphatidylserines 110-128 myristoylated alanine rich protein kinase C substrate Homo sapiens 10-14 17384256-2 2006 Annexin-V-MACS is able to separate apoptotic from nonapoptotic sperm on the basis of their externalization of phosphatidylserine (EPS). eps 130-133 myristoylated alanine rich protein kinase C substrate Homo sapiens 10-14 16941482-4 2006 The decrease in P-MARCKS induced by IGF-I was blocked by pretreatment of cells with phosphoinositide 3-kinase (PI3K) inhibitors, LY294002 and wortmannin. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one 129-137 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-24 16941482-4 2006 The decrease in P-MARCKS induced by IGF-I was blocked by pretreatment of cells with phosphoinositide 3-kinase (PI3K) inhibitors, LY294002 and wortmannin. Wortmannin 142-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-24 16941482-5 2006 A decrease in P-MARCKS was also observed in cells treated with a Rho-dependent kinase (ROCK) inhibitor, Y27632. Y 27632 104-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-22 17210631-0 2007 Quantitative proteomics analysis of human endothelial cell membrane rafts: evidence of MARCKS and MRP regulation in the sphingosine 1-phosphate-induced barrier enhancement. sphingosine 1-phosphate 120-143 myristoylated alanine rich protein kinase C substrate Homo sapiens 87-93 16868438-8 2006 In Cox regression models adjusted for age and established contributory markers in CCR5 and HLA class I genes, CTLA4-318T was associated with rapid progression to AIDS in MACS (relative hazard 1.69; 95% confidence interval, 1.15-2.49; P < 0.01) as opposed to a non-significant slower disease progression in ACS and no appreciable association in DCG. dcg 347-350 myristoylated alanine rich protein kinase C substrate Homo sapiens 170-174 16943556-6 2006 We also suggest the involvement of myristoylated alanine-rich C kinase substrate (MARCKS), which is known as a downstream target of PKC-epsilon, in ADP of LDCV exocytosis. Adenosine Diphosphate 148-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 35-80 16943556-6 2006 We also suggest the involvement of myristoylated alanine-rich C kinase substrate (MARCKS), which is known as a downstream target of PKC-epsilon, in ADP of LDCV exocytosis. Adenosine Diphosphate 148-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 16943556-6 2006 We also suggest the involvement of myristoylated alanine-rich C kinase substrate (MARCKS), which is known as a downstream target of PKC-epsilon, in ADP of LDCV exocytosis. ldcv 155-159 myristoylated alanine rich protein kinase C substrate Homo sapiens 35-80 16943556-6 2006 We also suggest the involvement of myristoylated alanine-rich C kinase substrate (MARCKS), which is known as a downstream target of PKC-epsilon, in ADP of LDCV exocytosis. ldcv 155-159 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 16943556-7 2006 The level of phospho-MARCKS correlated with the time course of ADP and was reduced by transfection with DN-PKC-epsilon. Adenosine Diphosphate 63-66 myristoylated alanine rich protein kinase C substrate Homo sapiens 21-27 16943556-9 2006 Furthermore, knockdown of MARCKS by siRNA resulted in inhibition of ADP and reduction of the number of fused vesicles. Adenosine Diphosphate 68-71 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 16943556-10 2006 Together, we provide evidence that ADP of LDCV exocytosis is regulated by PKC-epsilon and its downstream target MARCKS via modulating vesicle translocation. Adenosine Diphosphate 35-38 myristoylated alanine rich protein kinase C substrate Homo sapiens 112-118 16943556-10 2006 Together, we provide evidence that ADP of LDCV exocytosis is regulated by PKC-epsilon and its downstream target MARCKS via modulating vesicle translocation. ldcv 42-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 112-118 16677610-1 2006 It is well recognized that phorbol 12,13-dibutyrate (PDBu)-activated PKC directly phosphorylates myristoylated alanine-rich C kinase substrate (MARCKS), whose phosphorylation is used as a marker of PKC activation. Phorbol 12,13-Dibutyrate 27-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 97-142 16687208-10 2006 We further demonstrated MARCKS dissociation from actin after activation by ionomycin, a process that can lead to the breakdown of the actin network, thus allowing CGE. Ionomycin 75-84 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-30 16677610-1 2006 It is well recognized that phorbol 12,13-dibutyrate (PDBu)-activated PKC directly phosphorylates myristoylated alanine-rich C kinase substrate (MARCKS), whose phosphorylation is used as a marker of PKC activation. Phorbol 12,13-Dibutyrate 27-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 16677610-1 2006 It is well recognized that phorbol 12,13-dibutyrate (PDBu)-activated PKC directly phosphorylates myristoylated alanine-rich C kinase substrate (MARCKS), whose phosphorylation is used as a marker of PKC activation. Phorbol 12,13-Dibutyrate 53-57 myristoylated alanine rich protein kinase C substrate Homo sapiens 97-142 16677610-1 2006 It is well recognized that phorbol 12,13-dibutyrate (PDBu)-activated PKC directly phosphorylates myristoylated alanine-rich C kinase substrate (MARCKS), whose phosphorylation is used as a marker of PKC activation. Phorbol 12,13-Dibutyrate 53-57 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 16677610-2 2006 However, in SH-SY5Y neuroblastoma cells, Western blotting analyses revealed that Rho-associated coiled-coil kinase (ROCK)-specific inhibitor H-1152 inhibited PDBu-induced phosphorylation, and that a small G-protein inhibitor, toxin B, also inhibited MARCKS phosphorylation. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 141-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 250-256 16491014-7 2006 Histamine also phosphorylated PKC and myristoylated alanine-rich C kinase substrate. Histamine 0-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-83 16473140-3 2006 Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS). Platinum 79-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 237-282 16473140-3 2006 Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS). Platinum 79-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 284-290 16473140-3 2006 Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS). BBR 3464 96-103 myristoylated alanine rich protein kinase C substrate Homo sapiens 237-282 16473140-3 2006 Using display PCR, we found that acquisition of resistance to the multinuclear platinum complex BBR3464 was associated with modulation of several transcripts, including up-regulation of the major substrate of protein kinase C (PKC), the myristoylated alanine-rich C kinase substrate (MARCKS). BBR 3464 96-103 myristoylated alanine rich protein kinase C substrate Homo sapiens 284-290 15623535-4 2005 Small interfering RNA (siRNA) to MARCKS significantly inhibited, whereas overexpression of wild-type MARCKS significantly increased PMA-mediated NT secretion. Tetradecanoylphorbol Acetate 132-135 myristoylated alanine rich protein kinase C substrate Homo sapiens 101-107 16188227-2 2005 We recently demonstrated that continuous production of nitric oxide (NO) by neuronal NO synthase (nNOS) following phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS) and NMDA receptor NR2B subunits is essential for neuropathic pain. Nitric Oxide 55-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 133-187 16188227-7 2005 Phosphorylation of MARCKS and NADPH-diaphorase activity stimulated by the EP3 agonist were also blocked by H-1152. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 107-113 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 16341931-0 2005 Expression of MARCKS effector domain mutants alters phospholipase D activity and cytoskeletal morphology of SK-N-MC neuroblastoma cells. sk-n-mc 108-115 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 16341931-1 2005 Stable overexpression of myristoylated alanine-rich C-kinase substrate (MARCKS) is known to enhance phorbol ester stimulation of phospholipase D (PLD) activity and protein kinase Calpha (PKCalpha) levels in SK-N-MC neuroblastoma cells. Phorbol Esters 100-113 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 16341931-3 2005 Like control cells, those expressing wild type MARCKS were elongated and possessed longitudinally oriented stress fibers, although these cells were more prone to detach from the substratum and undergo cell death upon phorbol ester treatment. Phorbol Esters 217-230 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 15930268-5 2005 The impaired membrane binding is associated with this mutant"s inability to transduce several antitumorigenic signals as it fails to mediate phorbol ester-stimulated translocation of myristoylated alanine-rich protein kinase C substrate (MARCKS), to activate mitogen-activated protein kinase and to augment melatonin-stimulated neurite outgrowth. Phorbol Esters 141-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 183-236 15930268-5 2005 The impaired membrane binding is associated with this mutant"s inability to transduce several antitumorigenic signals as it fails to mediate phorbol ester-stimulated translocation of myristoylated alanine-rich protein kinase C substrate (MARCKS), to activate mitogen-activated protein kinase and to augment melatonin-stimulated neurite outgrowth. Phorbol Esters 141-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 238-244 16202710-3 2005 MARCKS associates with membranes via the combined action of myristoylation and a polybasic effector domain, which binds phospholipids and/or F-actin, unless phosphorylated by PKC. Phospholipids 120-133 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 15623535-5 2005 Endogenous MARCKS and green fluorescent protein-tagged wild-type MARCKS were translocated from membrane to cytosol upon PMA treatment, further confirming MARCKS activation. Tetradecanoylphorbol Acetate 120-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 11-17 15623535-5 2005 Endogenous MARCKS and green fluorescent protein-tagged wild-type MARCKS were translocated from membrane to cytosol upon PMA treatment, further confirming MARCKS activation. Tetradecanoylphorbol Acetate 120-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 15623535-5 2005 Endogenous MARCKS and green fluorescent protein-tagged wild-type MARCKS were translocated from membrane to cytosol upon PMA treatment, further confirming MARCKS activation. Tetradecanoylphorbol Acetate 120-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 15685354-6 2005 MACS reduced significantly the percentage of cryopreserved spermatozoa with dissipated mTMP to 8.1 +/- 3.9 (P <0.01) and also those with aCP to 9.3 % +/- 2.2 %. mtmp 87-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 15703821-9 2005 Furthermore, MARCKS was serine-phosphorylated in liver cirrhosis and HCC, and phosphorylated MARCKS was detected in a cytosolic fraction of these tissues. Serine 24-30 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 15765405-6 2005 DCA also caused dramatic translocation of PH-PLCdelta-GFP, and conventional, Ca2+/diacylglycerol (DAG)-dependent isoforms of PKC (PKC-betaI and PKC-alpha), and MARCKS-GFP, but only in Ca2+-containing solutions. Deoxycholic Acid 0-3 myristoylated alanine rich protein kinase C substrate Homo sapiens 160-166 15649142-9 2005 Thus MARCKS can act as a reversible PtdIns(4,5)P(2) buffer, binding PtdIns(4,5)P(2) in a quiescent cell, and releasing it locally when the intracellular Ca(2+) concentration increases. Phosphatidylinositol 4,5-Diphosphate 36-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 5-11 15703821-10 2005 In a phosphorylation study using the HLF HCC cell line, MARCKS was displaced from the plasma membrane to the cytosol following the activation of protein kinase C (PKC) by phorbol 12-myristrate 13-acetate (PMA). phorbol 12-myristrate 13-acetate 171-203 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 15703821-10 2005 In a phosphorylation study using the HLF HCC cell line, MARCKS was displaced from the plasma membrane to the cytosol following the activation of protein kinase C (PKC) by phorbol 12-myristrate 13-acetate (PMA). Tetradecanoylphorbol Acetate 205-208 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 15358594-10 2005 In response to carbachol, MARCKS translocates to the cytosol, indicating its phosphorylation, which is additionally confirmed biochemically. Carbachol 15-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 15358594-11 2005 Consistent with this observation, carbachol induces the translocation of PKC-epsilon to proximity with MARCKS at the lateral membrane. Carbachol 34-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 103-109 15607731-4 2005 In addition, possible degradation products of MARCKS were observed after transfection of PKG or stimulation with 8pCPT-cGMP. 8-((4-chlorophenyl)thio)cyclic-3',5'-GMP 113-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 46-52 15607731-5 2005 Western blot analysis showed that the MARCKS protein levels were decreased when the cells were stimulated with 8pCPT-cGMP. 8-((4-chlorophenyl)thio)cyclic-3',5'-GMP 111-121 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-44 15649142-9 2005 Thus MARCKS can act as a reversible PtdIns(4,5)P(2) buffer, binding PtdIns(4,5)P(2) in a quiescent cell, and releasing it locally when the intracellular Ca(2+) concentration increases. Phosphatidylinositol 4,5-Diphosphate 68-83 myristoylated alanine rich protein kinase C substrate Homo sapiens 5-11 15541367-6 2004 Translocation of MARCKS-GFP induced by VEGF-KDR stimulus was blocked by rottlerin, a PKCdelta specific inhibitor, or human PKCdelta siRNA. rottlerin 72-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 15708490-2 2005 A phosphorylation-site specific antibody against Ser159-phospho-MARCKS (pS159-Mar-Ab) revealed that MARCKS is phosphorylated at Ser159 by Rho-kinase and that its phosphorylation is inhibited by the Rho-kinase specific inhibitor H-1152. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 228-234 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 15708490-2 2005 A phosphorylation-site specific antibody against Ser159-phospho-MARCKS (pS159-Mar-Ab) revealed that MARCKS is phosphorylated at Ser159 by Rho-kinase and that its phosphorylation is inhibited by the Rho-kinase specific inhibitor H-1152. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 228-234 myristoylated alanine rich protein kinase C substrate Homo sapiens 100-106 14747473-4 2004 Interestingly, PKCdelta is the most strongly phosphorylated isoform, and the preferential PKCdelta inhibitor rottlerin largely prevented EGF-induced phosphorylation of PKC substrates and MARCKS. rottlerin 109-118 myristoylated alanine rich protein kinase C substrate Homo sapiens 187-193 15458842-0 2004 Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines. N-Methylaspartate 66-70 myristoylated alanine rich protein kinase C substrate Homo sapiens 33-39 15458842-9 2004 Together these data suggest a model in which NMDA-induced spine collapse involves cathepsin B-like proteolysis of MARCKS, and possibly other proteins that regulate the actin-based cytoskeleton. N-Methylaspartate 45-49 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-120 15298909-2 2004 We used a well-characterized peptide corresponding to the basic effector domain of myristoylated alanine-rich C kinase substrate, MARCKS(151-175), that was fluorescently labeled with Alexa488, and measured its binding to large unilamellar vesicles (diameter approximately 100 nm) composed of phosphatidylcholine and phosphatidylserine or phosphatidylinositol 4,5-bisphosphate. alexa488 183-191 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 15298909-2 2004 We used a well-characterized peptide corresponding to the basic effector domain of myristoylated alanine-rich C kinase substrate, MARCKS(151-175), that was fluorescently labeled with Alexa488, and measured its binding to large unilamellar vesicles (diameter approximately 100 nm) composed of phosphatidylcholine and phosphatidylserine or phosphatidylinositol 4,5-bisphosphate. Phosphatidylcholines 292-311 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 15298909-2 2004 We used a well-characterized peptide corresponding to the basic effector domain of myristoylated alanine-rich C kinase substrate, MARCKS(151-175), that was fluorescently labeled with Alexa488, and measured its binding to large unilamellar vesicles (diameter approximately 100 nm) composed of phosphatidylcholine and phosphatidylserine or phosphatidylinositol 4,5-bisphosphate. Phosphatidylserines 316-334 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 15298909-2 2004 We used a well-characterized peptide corresponding to the basic effector domain of myristoylated alanine-rich C kinase substrate, MARCKS(151-175), that was fluorescently labeled with Alexa488, and measured its binding to large unilamellar vesicles (diameter approximately 100 nm) composed of phosphatidylcholine and phosphatidylserine or phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 338-375 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 15189357-11 2004 This dynamic regulation was also observed at the level of PKC activation indicated by an enhanced translocation of eGFP-tagged myristoylated alanine-rich C kinase substrate (MARCKS) protein in cells stimulated with MCH. Methacholine Chloride 215-218 myristoylated alanine rich protein kinase C substrate Homo sapiens 174-180 15147504-5 2004 The results also demonstrate that rasagiline treatment significantly elevated the levels of phosphorylated myristoylated alanine-rich C kinase substrate (p-MARCKS), a major substrate for PKC, as well as the levels of receptors for activated C kinase 1 (RACK1). rasagiline 34-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-152 15147504-5 2004 The results also demonstrate that rasagiline treatment significantly elevated the levels of phosphorylated myristoylated alanine-rich C kinase substrate (p-MARCKS), a major substrate for PKC, as well as the levels of receptors for activated C kinase 1 (RACK1). rasagiline 34-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 156-162 15052337-0 2004 The MARCKS family of phospholipid binding proteins: regulation of phospholipase D and other cellular components. Phospholipids 21-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-10 15041641-5 2004 In agreement with experiments, we find that the electrostatic free energy becomes more favorable when: 1), Lys-13 and FA-MARCKS(151-175) sequester several PI(4,5)P2; 2), the linear charge density of the basic peptide increases; 3), the mol percent monovalent acidic lipid in the membrane decreases; and 4), the ionic strength of the solution decreases. (4,5)p2 157-164 myristoylated alanine rich protein kinase C substrate Homo sapiens 121-127 15041659-2 2004 Our working hypothesis is that the effector domain of MARCKS reversibly sequesters a significant fraction of the L-alpha-phosphatidyl-D-myo-inositol 4,5-bisphosphate (PIP2) on the plasma membrane. l-alpha-phosphatidyl-d-myo-inositol 4,5-bisphosphate 113-165 myristoylated alanine rich protein kinase C substrate Homo sapiens 54-60 15041659-2 2004 Our working hypothesis is that the effector domain of MARCKS reversibly sequesters a significant fraction of the L-alpha-phosphatidyl-D-myo-inositol 4,5-bisphosphate (PIP2) on the plasma membrane. Phosphatidylinositol 4,5-Diphosphate 167-171 myristoylated alanine rich protein kinase C substrate Homo sapiens 54-60 15041659-3 2004 To test this, we utilize three techniques that measure the ability of a peptide corresponding to its effector domain, MARCKS(151-175), to sequester PIP2 in model membranes containing physiologically relevant fractions (15-30%) of the monovalent acidic lipid phosphatidylserine. Phosphatidylinositol 4,5-Diphosphate 148-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 118-124 15041659-4 2004 First, we measure fluorescence resonance energy transfer from Bodipy-TMR-PIP2 to Texas Red MARCKS(151-175) adsorbed to large unilamellar vesicles. bodipy-tmr-pip2 62-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 91-97 15041659-4 2004 First, we measure fluorescence resonance energy transfer from Bodipy-TMR-PIP2 to Texas Red MARCKS(151-175) adsorbed to large unilamellar vesicles. Texas red 81-90 myristoylated alanine rich protein kinase C substrate Homo sapiens 91-97 15041659-5 2004 Second, we detect quenching of Bodipy-TMR-PIP2 in large unilamellar vesicles when unlabeled MARCKS(151-175) binds to vesicles. bodipy-tmr-pip2 31-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 92-98 15041659-6 2004 Third, we identify line broadening in the electron paramagnetic resonance spectra of spin-labeled PIP2 as unlabeled MARCKS(151-175) adsorbs to vesicles. Phosphatidylinositol 4,5-Diphosphate 98-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 116-122 15041641-4 2004 Here, we use the finite difference Poisson-Boltzmann method to test this hypothesis by calculating the electrostatic free energy of lateral sequestration of PI(4,5)P2 by membrane-adsorbed basic peptides: Lys-7, Lys-13, and FA-MARCKS(151-175), a peptide based on MARCKS(151-175). pi(4,5)p2 157-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 226-232 15041641-4 2004 Here, we use the finite difference Poisson-Boltzmann method to test this hypothesis by calculating the electrostatic free energy of lateral sequestration of PI(4,5)P2 by membrane-adsorbed basic peptides: Lys-7, Lys-13, and FA-MARCKS(151-175), a peptide based on MARCKS(151-175). pi(4,5)p2 157-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 262-268 15052337-2 2004 The most prominent structural feature of MARCKS and MRP is a central basic effector domain (ED) that binds F-actin, Ca2+-calmodulin, and acidic phospholipids; phosphorylation of key serine residues within the ED by protein kinase C (PKC) prevents the above interactions. Phospholipids 144-157 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-47 15052337-2 2004 The most prominent structural feature of MARCKS and MRP is a central basic effector domain (ED) that binds F-actin, Ca2+-calmodulin, and acidic phospholipids; phosphorylation of key serine residues within the ED by protein kinase C (PKC) prevents the above interactions. Serine 182-188 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-47 15052337-3 2004 While the precise roles of MARCKS and MRP have not been established, recent attention has focussed on the high affinity of the MARCKS ED for phosphatidylinositol 4,5-bisphosphate (PIP2), and a model has emerged in which calmodulin- or PKC-mediated regulation of these proteins at specific membrane sites could in turn control spatial availability of PIP2. Phosphatidylinositol 4,5-Diphosphate 141-178 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 15052337-3 2004 While the precise roles of MARCKS and MRP have not been established, recent attention has focussed on the high affinity of the MARCKS ED for phosphatidylinositol 4,5-bisphosphate (PIP2), and a model has emerged in which calmodulin- or PKC-mediated regulation of these proteins at specific membrane sites could in turn control spatial availability of PIP2. Phosphatidylinositol 4,5-Diphosphate 180-184 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 15052337-3 2004 While the precise roles of MARCKS and MRP have not been established, recent attention has focussed on the high affinity of the MARCKS ED for phosphatidylinositol 4,5-bisphosphate (PIP2), and a model has emerged in which calmodulin- or PKC-mediated regulation of these proteins at specific membrane sites could in turn control spatial availability of PIP2. Phosphatidylinositol 4,5-Diphosphate 350-354 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 15052337-4 2004 The present review summarizes recent progress in this area and discusses how the above model might explain a role for MARCKS and MRP in activation of phospholipase D and other PIP2-dependent cellular processes. Phosphatidylinositol 4,5-Diphosphate 176-180 myristoylated alanine rich protein kinase C substrate Homo sapiens 118-124 12670959-2 2003 Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity. Phenylalanine 137-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-15 13679307-4 2004 Isoform activity was demonstrated by cytosol-to-membrane translocation after PMA treatment and phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein after PMA and DAG treatment. Diglycerides 195-198 myristoylated alanine rich protein kinase C substrate Homo sapiens 118-163 13679307-4 2004 Isoform activity was demonstrated by cytosol-to-membrane translocation after PMA treatment and phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein after PMA and DAG treatment. Diglycerides 195-198 myristoylated alanine rich protein kinase C substrate Homo sapiens 165-171 13679307-7 2004 Furthermore, antisense treatment and pharmacological studies indicated that the novel isoform PKCdelta and PKD are both required for PMA- and DAG-induced MARCKS phosphorylation and hyperpermeability in pulmonary microvascular endothelial cells, whereas isoforms alpha, betaI, and epsilon were dispensable with regard to these same phenomena. Diglycerides 142-145 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 14501149-2 2003 Recently, it is considered that MARCKS is implicated in some neuronal functions, such as synaptic vesicle trafficking and neurotransmitter release, through regulation of the actin-containing cytoskeletal structure; this is based on the experimental results with short-term or prolonged pretreatment with phorbol esters and treatment by protein kinase C (PKC) inhibitor. Phorbol Esters 304-318 myristoylated alanine rich protein kinase C substrate Homo sapiens 32-38 14501149-4 2003 Recently, we have demonstrated that MARCKS is phosphorylated at Ser159 in PSD by Rho-kinase in vitro and that the phosphorylation occurred in neuronal cells upon stimulation with lysophosphatidic acid (LPA), and its phosphorylation was inhibited by a novel and specific Rho-kinase inhibitor, H-1152. lysophosphatidic acid 179-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 14501149-4 2003 Recently, we have demonstrated that MARCKS is phosphorylated at Ser159 in PSD by Rho-kinase in vitro and that the phosphorylation occurred in neuronal cells upon stimulation with lysophosphatidic acid (LPA), and its phosphorylation was inhibited by a novel and specific Rho-kinase inhibitor, H-1152. lysophosphatidic acid 202-205 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 14501149-4 2003 Recently, we have demonstrated that MARCKS is phosphorylated at Ser159 in PSD by Rho-kinase in vitro and that the phosphorylation occurred in neuronal cells upon stimulation with lysophosphatidic acid (LPA), and its phosphorylation was inhibited by a novel and specific Rho-kinase inhibitor, H-1152. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 292-298 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 14501149-5 2003 Our results allow us to speculate that a preinflammatory substance, such as LPA, interleukin 1-beta, and bradykinin, augments MARCKS phosphorylation in a novel signal transduction pathway besides the PKC-involved one, and thereby induces the release of a neurotransmitter through a reorganization of actin-containing microfilaments at the cell periphery, the so-called "active zone". lysophosphatidic acid 76-79 myristoylated alanine rich protein kinase C substrate Homo sapiens 126-132 14506265-2 2003 Although we have previously observed that myristoylated and non-myristoylated MARCKS proteins behave differently during calmodulin-agarose chromatography, the role of protein myristoylation in the MARCKS-calmodulin interaction remained to be elucidated. Sepharose 131-138 myristoylated alanine rich protein kinase C substrate Homo sapiens 78-84 14506265-4 2003 Both myristoylated and non-myristoylated recombinant MARCKS bound to calmodulin-agarose at low ionic strengths, but only the former retained the affinity at high ionic strengths. Sepharose 80-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 14507707-0 2003 Location of the myristoylated alanine-rich C-kinase substrate (MARCKS) effector domain in negatively charged phospholipid bicelles. Phospholipids 109-121 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-70 14507707-3 2003 Here, the position of the MARCKS-ED was determined when bound to phospholipid bicelles using high-resolution NMR methods. Phospholipids 65-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 14507707-4 2003 Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned within the membrane hydrocarbon a few angstroms from the aqueous-hydrocarbon interface. Phenylalanine 35-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 14507707-4 2003 Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned within the membrane hydrocarbon a few angstroms from the aqueous-hydrocarbon interface. Hydrocarbons 110-121 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 14507707-4 2003 Two sets of data indicate that the phenylalanine residues of the MARCKS-ED are positioned within the membrane hydrocarbon a few angstroms from the aqueous-hydrocarbon interface. Hydrocarbons 155-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 14507707-8 2003 These results indicate that highly charged peptides such as the MARCKS-ED penetrate the membrane interface with aromatic amino acid side chains inserted into the hydrocarbon and the peptide backbone lying within the bilayer interface. Amino Acids, Aromatic 112-131 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 14507707-8 2003 These results indicate that highly charged peptides such as the MARCKS-ED penetrate the membrane interface with aromatic amino acid side chains inserted into the hydrocarbon and the peptide backbone lying within the bilayer interface. Hydrocarbons 162-173 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 14507707-9 2003 This position may serve to enhance the electrostatic fields produced by this basic domain at the membrane interface and may play a role in the ability of the MARCKS-ED to sequester polyphosphoinositides. Phosphatidylinositol Phosphates 181-202 myristoylated alanine rich protein kinase C substrate Homo sapiens 158-164 12670959-0 2003 Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. Phenylalanine 75-88 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-141 12670959-1 2003 Electrostatic interactions with positively charged regions of membrane-associated proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) may have a role in regulating the level of free phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in plasma membranes. Phosphatidylinositol 4,5-Diphosphate 202-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 99-144 12670959-1 2003 Electrostatic interactions with positively charged regions of membrane-associated proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) may have a role in regulating the level of free phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in plasma membranes. Phosphatidylinositol 4,5-Diphosphate 202-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 12670959-1 2003 Electrostatic interactions with positively charged regions of membrane-associated proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) may have a role in regulating the level of free phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in plasma membranes. pi(4,5)p2 241-250 myristoylated alanine rich protein kinase C substrate Homo sapiens 99-144 12670959-1 2003 Electrostatic interactions with positively charged regions of membrane-associated proteins such as myristoylated alanine-rich C kinase substrate (MARCKS) may have a role in regulating the level of free phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) in plasma membranes. pi(4,5)p2 241-250 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 12670959-2 2003 Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity. Phenylalanine 137-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 12670959-2 2003 Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity. pi(4,5)p2 213-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-15 12670959-2 2003 Both the MARCKS protein and a peptide corresponding to the effector domain (an unstructured region that contains 13 basic residues and 5 phenylalanines), MARCKS-(151-175), laterally sequester the polyvalent lipid PI(4,5)P2 in the plane of a bilayer membrane with high affinity. pi(4,5)p2 213-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 12670959-4 2003 Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2. Phenylalanine 137-140 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 12670959-4 2003 Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2. Phosphatidylcholines 207-226 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 12670959-4 2003 Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2. Phosphatidylglycerols 247-267 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 12670959-4 2003 Measurements of cross-relaxation rates in two-dimensional nuclear Overhauser enhancement spectroscopy NMR experiments show that the five Phe rings of MARCKS-(151-175) penetrate into the acyl chain region of phosphatidylcholine bilayers containing phosphatidylglycerol or PI(4,5)P2. pi(4,5)p2 271-280 myristoylated alanine rich protein kinase C substrate Homo sapiens 150-156 12670959-7 2003 The deep location of the MARCKS peptide in the polar head group region should enhance its electrostatic sequestration of PI(4,5)P2 by an "image charge" mechanism. pi(4,5)p2 121-130 myristoylated alanine rich protein kinase C substrate Homo sapiens 25-31 12417254-6 2002 Furthermore, the use of bisindolylmaleimide (BIM), a non-selective PKC inhibitor, serves to demonstrate the specificity of the PKC-dependent MARCKS-psd phosphorylation. bisindolylmaleimide 24-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 141-147 12623878-8 2003 Nuclei isolated from undifferentiated cells were able to phosphorylate the acrylodan-labeled MARCKS peptide, a high-affinity fluorescent PKC substrate. acrylodan 75-84 myristoylated alanine rich protein kinase C substrate Homo sapiens 93-99 12629049-5 2003 Because PKCalpha can phosphorylate the myristoylated alanine-rich C-kinase substrate (MARCKS) motif of DGKzeta, we tested whether this modification could affect their interaction. Alanine 53-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 86-92 12417254-6 2002 Furthermore, the use of bisindolylmaleimide (BIM), a non-selective PKC inhibitor, serves to demonstrate the specificity of the PKC-dependent MARCKS-psd phosphorylation. bisindolylmaleimide 45-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 141-147 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Glycine 89-92 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Alanine 93-96 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Alanine 117-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Glutamine 97-100 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Arginine 121-124 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 105-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Arginine 125-128 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Lysine 109-112 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Glycine 196-199 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Asparagine 200-203 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Alanine 117-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 208-211 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Serine 208-211 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Lysine 220-223 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Lysine 220-223 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Lysine 220-223 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12417259-5 2002 When a MARCKS (myristoylated alanine-rich C-kinase substrate)-derived peptide substrate (Gly-Ala-Gln-Phe-Ser-Lys-Thr-Ala-Arg-Arg) and the M2 gene segment of the reovirus type 3 peptide substrate (Gly-Asn-Ala-Ser-Ser-Ile-Lys-Lys-Lys) were used, hNMT activity was increased by approximately 8.5- and 7-fold, respectively. Threonine 113-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 12137567-6 2002 In the present study, MRP cleavage was used as an assay to measure the capacity of various MRP or MARCKS ED peptides to block gp63 activity. Peptides 108-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 98-104 12417259-6 2002 Dimethyl sulfone (20%) increased hNMT activity between 2.5- and 3.5-fold in the presence of pp60(src), MARCKS, and M2 gene segment peptides. dimethyl sulfone 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 103-109 12417259-7 2002 Dimethyl formamide (20%) increased the hNMT activity by 8.5-, 8.5-, 5.5- and 3.5-fold when pp60(src), MARCKS, M2, and cAMP-dependent protein kinase-derived peptide substrates were used, respectively. Dimethylformamide 0-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 102-108 12045217-3 2002 Treatment with okadaic acid or tautomycin, which are potent inhibitors of protein phosphatases and cell fusion, was found to reversibly block the MARCKS translocation. Okadaic Acid 15-27 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 12045217-3 2002 Treatment with okadaic acid or tautomycin, which are potent inhibitors of protein phosphatases and cell fusion, was found to reversibly block the MARCKS translocation. tautomycin 31-41 myristoylated alanine rich protein kinase C substrate Homo sapiens 146-152 11937071-6 2002 Inhibition of PKC with the PKC-selective inhibitor, LY333531, prevented the VPA-induced down-regulation of membrane-associated MARCKS, but had no effect on the cytosolic MARCKS reduction or the GAP-43 up-regulation. Valproic Acid 76-79 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 11937071-2 2002 In the present study we have examined the effects of VPA on the expression of two prominent substrates for protein kinase C (PKC) in the brain, MARCKS and GAP-43, which have been implicated in actin-membrane plasticity and neurite outgrowth during neuronal differentiation, respectively, and are essential to normal brain development. Valproic Acid 53-56 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 11937071-8 2002 Collectively, these data indicate that VPA induces neuronal differentiation, associated with a reduction in MARCKS expression and an increase in GAP-43 expression, consistent with the hypothesis that a reduction in MARCKS at the membrane may be permissive for cytoskeletal plasticity during neurite outgrowth. Valproic Acid 39-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 11937071-8 2002 Collectively, these data indicate that VPA induces neuronal differentiation, associated with a reduction in MARCKS expression and an increase in GAP-43 expression, consistent with the hypothesis that a reduction in MARCKS at the membrane may be permissive for cytoskeletal plasticity during neurite outgrowth. Valproic Acid 39-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 215-221 11327693-2 2001 We found that PMA-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) increased its binding with Tob that exerts an anti-proliferative effect through the binding with ErbB-2. Tetradecanoylphorbol Acetate 14-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-90 11937071-6 2002 Inhibition of PKC with the PKC-selective inhibitor, LY333531, prevented the VPA-induced down-regulation of membrane-associated MARCKS, but had no effect on the cytosolic MARCKS reduction or the GAP-43 up-regulation. ruboxistaurin 52-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 11825894-6 2002 This result indicates that at least some proxyl-PIP(2) are in close proximity when bound to MARCKS and that MARCKS associates with multiple PI(4,5)P(2) molecules. pi(4,5)p 140-148 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 11825894-7 2002 Titration of the proxyl-PIP(2) EPR signal by the MARCKS-derived peptide also suggests that multiple PI(4,5)P(2) molecules interact with MARCKS. pi(4,5)p 100-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 11825894-7 2002 Titration of the proxyl-PIP(2) EPR signal by the MARCKS-derived peptide also suggests that multiple PI(4,5)P(2) molecules interact with MARCKS. pi(4,5)p 100-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 136-142 11825894-9 2002 These data are consistent with the hypothesis that MARCKS functions to sequester multiple PI(4,5)P(2) molecules within the plane of the membrane as a result of interactions that are driven by electrostatic forces. pi(4,5)p 90-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 12067241-0 2002 Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 131-137 myristoylated alanine rich protein kinase C substrate Homo sapiens 33-78 12067241-0 2002 Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 131-137 myristoylated alanine rich protein kinase C substrate Homo sapiens 80-86 12067241-4 2002 H-1152 dose-dependently inhibited the phosphorylation of MARCKS in human neuroteratoma (NT-2) cells stimulated by Rho-activator lysophosphatidic acid (LPA), which was determined by phosphorylation site-specific antibody against phospho-Ser159 in MARCKS, whereas it hardly inhibited the phosphorylation stimulated by phorbol-12,13-dibutyrate (PDBu). lysophosphatidic acid 128-149 myristoylated alanine rich protein kinase C substrate Homo sapiens 57-63 12067241-4 2002 H-1152 dose-dependently inhibited the phosphorylation of MARCKS in human neuroteratoma (NT-2) cells stimulated by Rho-activator lysophosphatidic acid (LPA), which was determined by phosphorylation site-specific antibody against phospho-Ser159 in MARCKS, whereas it hardly inhibited the phosphorylation stimulated by phorbol-12,13-dibutyrate (PDBu). lysophosphatidic acid 151-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 57-63 12067241-4 2002 H-1152 dose-dependently inhibited the phosphorylation of MARCKS in human neuroteratoma (NT-2) cells stimulated by Rho-activator lysophosphatidic acid (LPA), which was determined by phosphorylation site-specific antibody against phospho-Ser159 in MARCKS, whereas it hardly inhibited the phosphorylation stimulated by phorbol-12,13-dibutyrate (PDBu). Phorbol 12,13-Dibutyrate 316-340 myristoylated alanine rich protein kinase C substrate Homo sapiens 57-63 12067241-4 2002 H-1152 dose-dependently inhibited the phosphorylation of MARCKS in human neuroteratoma (NT-2) cells stimulated by Rho-activator lysophosphatidic acid (LPA), which was determined by phosphorylation site-specific antibody against phospho-Ser159 in MARCKS, whereas it hardly inhibited the phosphorylation stimulated by phorbol-12,13-dibutyrate (PDBu). Phorbol 12,13-Dibutyrate 342-346 myristoylated alanine rich protein kinase C substrate Homo sapiens 57-63 12067241-5 2002 In contrast, two other Rho-kinase inhibitors, HA-1077 at 30 microM and Y-27632 at 10-30 microM, inhibited the phosphorylation of MARCKS in the cells stimulated by LPA and PDBu. histidinoalanine 46-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 129-135 12067241-5 2002 In contrast, two other Rho-kinase inhibitors, HA-1077 at 30 microM and Y-27632 at 10-30 microM, inhibited the phosphorylation of MARCKS in the cells stimulated by LPA and PDBu. Y 27632 71-78 myristoylated alanine rich protein kinase C substrate Homo sapiens 129-135 12067241-5 2002 In contrast, two other Rho-kinase inhibitors, HA-1077 at 30 microM and Y-27632 at 10-30 microM, inhibited the phosphorylation of MARCKS in the cells stimulated by LPA and PDBu. lysophosphatidic acid 163-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 129-135 12067241-6 2002 A PKC inhibitor Ro-31-8220 selectively inhibited PDBu-induced phosphorylation of MARCKS. Ro 31-8220 16-26 myristoylated alanine rich protein kinase C substrate Homo sapiens 81-87 12067241-7 2002 Taken together with our previous results, the present findings strongly suggest that Rho/Rho-kinase phosphorylates MARCKS at Ser159 residue in neuronal cells in response to LPA stimulation and that H-1152 is a useful tool to confirm Rho-kinase function(s) in cells and tissues. lysophosphatidic acid 173-176 myristoylated alanine rich protein kinase C substrate Homo sapiens 115-121 11806947-2 2002 The two signals compete for the same domains in certain substrates, such as myristoylated alanine-rich PKC-substrate (MARCKS). Alanine 90-97 myristoylated alanine rich protein kinase C substrate Homo sapiens 118-124 11882609-7 2002 This translocation was blocked by an antisense oligonucleotide to PKCbeta and MARCKS. Oligonucleotides 47-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 78-84 12191614-6 2002 This inhibitor suppressed the phosphorylation of myristoylated alanine-rich C-kinase substance (MARCKS) in neuronal cells stimulated with lysophosphatidic acid, whose phosphorylation site was confirmed to be the Ser159 residue, using a phosphorylation site-specific antibody. lysophosphatidic acid 138-159 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 12191614-7 2002 In contrast, phorbol 12-myristate 13-acetate-induced phosphorylation of MARCKS was scarcely inhibited by H-1152P. Tetradecanoylphorbol Acetate 13-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 12191614-7 2002 In contrast, phorbol 12-myristate 13-acetate-induced phosphorylation of MARCKS was scarcely inhibited by H-1152P. 2-methyl-1-((4-methyl-5-isoquinolinyl)sulfonyl)homopiperazine 105-112 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 11377822-2 2001 The purpose of this study is to explore ANP-induced changes in the phosphorylation of myristoylated alanine-rich C-kinase substrate (MARCKS) and the steroidogenic acute regulatory protein (StAR), in AngII or K(+)-stimulated glomerulosa cells. Alanine 100-107 myristoylated alanine rich protein kinase C substrate Homo sapiens 133-139 11825894-0 2002 Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. Phosphatidylinositol 4,5-Diphosphate 79-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 11825894-0 2002 Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. Phosphatidylinositol 4,5-Diphosphate 79-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 11825894-1 2002 The myristoylated alanine-rich protein kinase C substrate (MARCKS) may function to sequester phosphoinositides within the plane of the bilayer. Phosphatidylinositols 93-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-57 11825894-1 2002 The myristoylated alanine-rich protein kinase C substrate (MARCKS) may function to sequester phosphoinositides within the plane of the bilayer. Phosphatidylinositols 93-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 59-65 11825894-6 2002 This result indicates that at least some proxyl-PIP(2) are in close proximity when bound to MARCKS and that MARCKS associates with multiple PI(4,5)P(2) molecules. proxyl-pip 41-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 92-98 11988466-5 2002 We conclude by considering the hypothesis that proteins such as MARCKS bind a significant fraction of the PIP2 in a cell, helping to sequester it in lateral membrane domains, then release this lipid in response to local signals such as an increased concentration of Ca(++)/calmodulin or activation of protein kinase C. Phosphatidylinositol 4,5-Diphosphate 106-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 11477066-7 2001 In intact or permeabilized cells MARCKS phosphorylation increased upon stimulation with 10(-7) m phorbol 12-myristate 13-acetate. Tetradecanoylphorbol Acetate 97-128 myristoylated alanine rich protein kinase C substrate Homo sapiens 33-39 11477066-12 2001 These results provide the first evidence for MARCKS involvement in chromaffin cell secretion and suggest that regulation of cortical F-actin cross-linking might be involved in this process. chromaffin 67-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-51 11327693-2 2001 We found that PMA-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) increased its binding with Tob that exerts an anti-proliferative effect through the binding with ErbB-2. Tetradecanoylphorbol Acetate 14-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 92-98 11260059-0 2001 Myristoylated alanine-rich C kinase substrate phosphorylation is involved in thrombin-induced serotonin release from platelets. Serotonin 94-103 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 11260059-2 2001 Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) and serotonin release in intact and digitonin-permeabilized platelets. Digitonin 195-204 myristoylated alanine rich protein kinase C substrate Homo sapiens 104-149 11260059-2 2001 Here, we demonstrate that, in human platelets, thrombin stimulation also induced phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) and serotonin release in intact and digitonin-permeabilized platelets. Digitonin 195-204 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 11264665-0 2001 Overexpression of the myristoylated alanine-rich C kinase substrate decreases uptake and K(+)-evoked release of noradrenaline in the human neuroblastoma SH-SY5Y. Norepinephrine 112-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 22-67 11264665-1 2001 The aim of this study was to investigate a possible role of the myristoylated alanine-rich C kinase substrate (MARCKS) in the mechanism of noradrenaline uptake and release in the human neuroblastoma cell line SH-SY5Y. Norepinephrine 139-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-109 11264665-1 2001 The aim of this study was to investigate a possible role of the myristoylated alanine-rich C kinase substrate (MARCKS) in the mechanism of noradrenaline uptake and release in the human neuroblastoma cell line SH-SY5Y. Norepinephrine 139-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 111-117 11264665-2 2001 A stable cell line showing a twofold overexpression of MARCKS was prepared by transfecting SH-SY5Y with pCEP4 containing MARCKS cDNA in the sense orientation. pcep4 104-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 55-61 11264665-2 2001 A stable cell line showing a twofold overexpression of MARCKS was prepared by transfecting SH-SY5Y with pCEP4 containing MARCKS cDNA in the sense orientation. pcep4 104-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 121-127 11264665-5 2001 In contrast, specific uptake and depolarization-evoked (100 mM K(+)) release of noradrenaline from the cell line overexpressing MARCKS was inhibited by approximately 50% compared with mock-transfected SH-SY5Y. Norepinephrine 80-93 myristoylated alanine rich protein kinase C substrate Homo sapiens 128-134 11264665-8 2001 Thus, in SH-SY5Y cells, overexpression of MARCKS leads to a decrease in the K(+)-evoked noradrenaline release possibly by increased actin cross-linking preventing the movement of noradrenaline containing large dense-cored vesicles to the plasma membrane in response to depolarization. Norepinephrine 88-101 myristoylated alanine rich protein kinase C substrate Homo sapiens 42-48 11264665-8 2001 Thus, in SH-SY5Y cells, overexpression of MARCKS leads to a decrease in the K(+)-evoked noradrenaline release possibly by increased actin cross-linking preventing the movement of noradrenaline containing large dense-cored vesicles to the plasma membrane in response to depolarization. Norepinephrine 179-192 myristoylated alanine rich protein kinase C substrate Homo sapiens 42-48 11053422-0 2001 The effector domain of myristoylated alanine-rich C kinase substrate binds strongly to phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 87-124 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-68 11053422-7 2001 MARCKS-(151-175) binds equally well to PI(4,5)P(2) and PI(3,4)P(2). pi(4,5)p 39-47 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 11053422-7 2001 MARCKS-(151-175) binds equally well to PI(4,5)P(2) and PI(3,4)P(2). pi(3,4)p 55-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 11053422-8 2001 Local electrostatic interactions of PIP(2) with MARCKS-(151-175) contribute to the binding energy because increasing the salt concentration from 100 to 500 mm decreases the binding 100-fold. Salts 121-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 11054811-0 2000 Differential regulation of primary protein kinase C substrate (MARCKS, MLP, GAP-43, RC3) mRNAs in the hippocampus during kainic acid-induced seizures and synaptic reorganization. Kainic Acid 121-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 63-69 11162562-5 2001 In human neuronal teratoma (NT-2) cells, lysophosphatidic acid (LPA) induced MARCKS phosphorylation dose- and time-dependently. lysophosphatidic acid 41-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 11162562-5 2001 In human neuronal teratoma (NT-2) cells, lysophosphatidic acid (LPA) induced MARCKS phosphorylation dose- and time-dependently. lysophosphatidic acid 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 11162562-9 2001 These findings suggest that the Ser159 residue of MARCKS is a target of LPA-stimulated Rho-kinase in neuronal cells. lysophosphatidic acid 72-75 myristoylated alanine rich protein kinase C substrate Homo sapiens 50-56 11115359-12 2000 In contrast, MARCKS increased in the membrane in response to retinoic acid treatment. Tretinoin 61-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 11115359-13 2000 These data indicate that retinoid treatment causes inactivation of PKC-alpha, allowing MARCKS to relocalize to the membrane, where it can cross-link actin filaments. Retinoids 25-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 87-93 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Alanine 22-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 11018286-3 2000 In this report we show that macrophage extracts contain a protease which specifically cleaves human MARCKS, expressed in a cell-free system or in E. coli, between Lys-6 and Thr-7. Lysine 163-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 100-106 11018286-3 2000 In this report we show that macrophage extracts contain a protease which specifically cleaves human MARCKS, expressed in a cell-free system or in E. coli, between Lys-6 and Thr-7. Threonine 173-176 myristoylated alanine rich protein kinase C substrate Homo sapiens 100-106 10871043-0 2000 Regulation of the binding of myristoylated alanine-rich C kinase substrate (MARCKS) related protein to lipid bilayer membranes by calmodulin. Lipid Bilayers 103-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 29-74 10871043-0 2000 Regulation of the binding of myristoylated alanine-rich C kinase substrate (MARCKS) related protein to lipid bilayer membranes by calmodulin. Lipid Bilayers 103-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 76-82 10871043-1 2000 The effector domain (ED) of MARCKS proteins can associate with calmodulin (CaM) as well as with phospholipids. Phospholipids 96-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 10871043-2 2000 It is not clear, however, whether a complex between MARCKS proteins and CaM can form at the surface of phospholipid membranes or whether CaM and membranes compete for ED binding. Phospholipids 103-115 myristoylated alanine rich protein kinase C substrate Homo sapiens 52-58 10771116-0 2000 Modulation of calcium-evoked [3H]noradrenaline release from permeabilized cerebrocortical synaptosomes by the MARCKS protein, calmodulin and the actin cytoskeleton. Calcium 14-21 myristoylated alanine rich protein kinase C substrate Homo sapiens 110-116 10771116-0 2000 Modulation of calcium-evoked [3H]noradrenaline release from permeabilized cerebrocortical synaptosomes by the MARCKS protein, calmodulin and the actin cytoskeleton. [3h]noradrenaline 29-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 110-116 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). sk-n-mc 3-10 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-152 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). sk-n-mc 3-10 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). Phorbol Esters 38-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-152 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). Phorbol Esters 38-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). Tetradecanoylphorbol Acetate 53-56 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-152 11018470-2 2000 In SK-N-MC human neuroblastoma cells, phorbol ester (TPA) activation of PLD was enhanced by overexpressing myristoylated alanine-rich C kinase substrate (MARCKS). Tetradecanoylphorbol Acetate 53-56 myristoylated alanine rich protein kinase C substrate Homo sapiens 154-160 10956022-7 2000 Replacing the five Phe with five Ala residues in MARCKS(151-175) decreases the binding to 10:1 PC/PS vesicles only slightly (6-fold). Phenylalanine 19-22 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 10956022-7 2000 Replacing the five Phe with five Ala residues in MARCKS(151-175) decreases the binding to 10:1 PC/PS vesicles only slightly (6-fold). Alanine 33-36 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 10956022-9 2000 Incorporating multivalent phosphatidylinositol 4, 5-bisphosphate (PIP(2)) into PC vesicles produces dramatically different effects on the membrane binding of the two peptides: 1% PIP(2) enhances caveolin(92-101) binding only 3-fold, but increases MARCKS(151-175) binding 10(4)-fold. piperidine 66-69 myristoylated alanine rich protein kinase C substrate Homo sapiens 247-253 10956022-10 2000 The strong interaction between the effector region of MARCKS and PIP(2) has interesting implications for the cellular function of MARCKS. Phosphatidylinositol 4,5-Diphosphate 65-71 myristoylated alanine rich protein kinase C substrate Homo sapiens 54-60 10956022-10 2000 The strong interaction between the effector region of MARCKS and PIP(2) has interesting implications for the cellular function of MARCKS. Phosphatidylinositol 4,5-Diphosphate 65-71 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 10801334-6 2000 Spermine, polylysine, and MARCKS (151-175) peptide caused scrambling in parallel to their reported ability to form domains of acidic phospholipids, including PIP(2). Phospholipids 133-146 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Phenylalanine 232-246 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Phenylalanine 232-246 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 10736562-3 2000 MARCKS (and MRP) interact inter alia with lipid bilayer membranes (via the myristoyl group and the ED), with protein kinases (which phosphorylate the serines in the ED), and with calmodulin (via the ED); synergies between these diverse interactions present an unusually rich array of possibilities for a variety of regulatory roles. Serine 150-157 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Glutamic Acid 187-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Glutamic Acid 187-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Lysine 211-218 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Lysine 211-218 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Serine 220-227 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 10736562-1 2000 MARCKS (myristoylated alanine-rich C kinase substrate, 32 kDa) and its 20 kDa brother MARCKS-related protein (MRP) are abundant, widely distributed proteins unusually rich in alanine and glutamic acid, and with lysines, serines and phenylalanines concentrated in a compact "effector domain" (ED) near the middle of the sequence. Serine 220-227 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 10865122-10 2000 A peptide with amino acid sequence corresponding to the phosphorylation site domain of MARCKS, which also corresponds to its actin binding site, blocks PMA potentiation of Ca(2+)-induced catecholamine release. Catecholamines 187-200 myristoylated alanine rich protein kinase C substrate Homo sapiens 87-93 10209306-0 1999 Continuous phosphorylation of GAP-43 and MARCKS by long-term TPA treatment in SK-N-SH human neuroblastoma cells. Tetradecanoylphorbol Acetate 61-64 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-47 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Serotonin 163-172 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Serotonin 163-172 myristoylated alanine rich protein kinase C substrate Homo sapiens 106-112 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Serotonin 163-172 myristoylated alanine rich protein kinase C substrate Homo sapiens 106-112 10648401-6 2000 MARCKS phosphorylation and serotonin release from permeabilized platelets have the same time course and were blocked by a peptide (MPSD) with the amino acid sequence corresponding to the phosphorylation site domain of MARCKS. Serotonin 27-36 myristoylated alanine rich protein kinase C substrate Homo sapiens 218-224 10600776-7 1999 PMA induced membrane-to-cytosol redistribution of the F-actin cross-linking protein myristoylated alanine-rich C kinase substrate (MARCKS). Tetradecanoylphorbol Acetate 0-3 myristoylated alanine rich protein kinase C substrate Homo sapiens 131-137 10600776-8 1999 Cytochalasin D also induced MARCKS translocation and enhanced PMA-stimulated translocation of MARCKS. Cytochalasin D 0-14 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 10600776-8 1999 Cytochalasin D also induced MARCKS translocation and enhanced PMA-stimulated translocation of MARCKS. Cytochalasin D 0-14 myristoylated alanine rich protein kinase C substrate Homo sapiens 94-100 10537078-3 1999 We find that direct PKC activation with phorbol esters, K+-induced depolarization, and activation of metabotropic glutamate receptors increase the in situ phosphorylation of both MARCKS and GAP-43/B-50. Phorbol Esters 40-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 179-185 10209246-6 1999 At short times of incubation with 1 mM Cch, a concentration which maximally activates PI metabolism, increased phosphorylation of a group of synaptosomal proteins, including B-50 and myristoylated, alanine-rich C kinase substrate (MARCKS), was observed. Carbachol 39-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 231-237 10209246-9 1999 Phosphorylation of B-50 and MARCKS was sensitive to Cch in both cases. Carbachol 52-55 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Phorbol Esters 30-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Phorbol Esters 30-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 106-112 10648401-0 2000 Platelet secretion induced by phorbol esters stimulation is mediated through phosphorylation of MARCKS: a MARCKS-derived peptide blocks MARCKS phosphorylation and serotonin release without affecting pleckstrin phosphorylation. Phorbol Esters 30-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 106-112 10622182-3 1999 Chronic lithium administration produces a reduction in the expression of PKC alpha and epsilon, as well as a major PKC substrate, MARCKS, which has been implicated in long-term neuroplastic events in the developing and adult brain. Lithium 8-15 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 10504221-3 1999 In the present study, the role of phenylanine in determining the membrane position, dynamics and free energy of a peptide derived from the effector domain of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein was examined. phenylanine 34-45 myristoylated alanine rich protein kinase C substrate Homo sapiens 162-207 10504221-3 1999 In the present study, the role of phenylanine in determining the membrane position, dynamics and free energy of a peptide derived from the effector domain of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein was examined. phenylanine 34-45 myristoylated alanine rich protein kinase C substrate Homo sapiens 209-215 10504221-4 1999 Deuterium NMR in membranes containing phosphatidylcholine (PC) and phosphatidylserine (PS) indicates that this peptide, MARCKS(151-175), partially penetrates the membrane interface when bound and alters the effective charge density on the membrane interface by approximately 2 charges per bound peptide. Deuterium 0-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 10504221-4 1999 Deuterium NMR in membranes containing phosphatidylcholine (PC) and phosphatidylserine (PS) indicates that this peptide, MARCKS(151-175), partially penetrates the membrane interface when bound and alters the effective charge density on the membrane interface by approximately 2 charges per bound peptide. Phosphatidylcholines 38-57 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 10504221-4 1999 Deuterium NMR in membranes containing phosphatidylcholine (PC) and phosphatidylserine (PS) indicates that this peptide, MARCKS(151-175), partially penetrates the membrane interface when bound and alters the effective charge density on the membrane interface by approximately 2 charges per bound peptide. Phosphatidylserines 67-85 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 10504221-4 1999 Deuterium NMR in membranes containing phosphatidylcholine (PC) and phosphatidylserine (PS) indicates that this peptide, MARCKS(151-175), partially penetrates the membrane interface when bound and alters the effective charge density on the membrane interface by approximately 2 charges per bound peptide. Phosphatidylserines 87-89 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 10504221-5 1999 However, a derivative of this peptide in which the five phenylalanines are replaced by alanine, MARCKS-Ala, does not penetrate the interface when membrane-bound. Alanine 103-106 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 10504221-9 1999 The side-chain dynamics of MARCKS-Ala are strongly influenced by membrane charge density and indicate that this peptide is drawn closer to the membrane interface at higher charge densities. Alanine 34-37 myristoylated alanine rich protein kinase C substrate Homo sapiens 27-33 10504221-10 1999 As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface. Alanine 20-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 10504221-10 1999 As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface. Phenylalanine 130-143 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 10504221-10 1999 As expected, MARCKS-Ala binds more weakly to membranes composed of PS/PC (1:9) than does the native MARCKS peptide; however, each phenylalanine contributes only 0.2 kcal/mol to the binding energy difference, far less than the 1.3 kcal/mol expected for the binding of phenylalanine to the membrane interface. Phenylalanine 267-280 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 10209306-3 1999 Cells were treated with 70 nM TPA for 15 min, 17 or 72 h. Phosphorylation of MARCKS and GAP-43 was elevated throughout 72 h of TPA. Tetradecanoylphorbol Acetate 30-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 10209306-3 1999 Cells were treated with 70 nM TPA for 15 min, 17 or 72 h. Phosphorylation of MARCKS and GAP-43 was elevated throughout 72 h of TPA. Tetradecanoylphorbol Acetate 127-130 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 10209306-4 1999 The magnitude and peptidic sites of phosphorylation in GAP-43 and MARCKS were similar after all TPA treatments. Tetradecanoylphorbol Acetate 96-99 myristoylated alanine rich protein kinase C substrate Homo sapiens 66-72 9990296-2 1999 Addition of [gamma-32P]ATP to the membrane fraction of digitonin-permeabilized C6 glioma cells resulted in phosphorylation and release of MARCKS, indicating involvement of an active membrane-bound kinase. [gamma-32p]atp 12-26 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-144 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). 2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide 104-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). 2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimide 104-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 202-208 9990296-2 1999 Addition of [gamma-32P]ATP to the membrane fraction of digitonin-permeabilized C6 glioma cells resulted in phosphorylation and release of MARCKS, indicating involvement of an active membrane-bound kinase. Digitonin 55-64 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-144 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). Egtazic Acid 232-236 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9990296-3 1999 Pretreatment of cells with 2 microM 4 beta-12-O-tetradecanoyl-phorbol-13-acetate (beta-TPA) for 18 h downregulated conventional (PKC alpha) and novel (PKC delta) isoforms of PKC by > 90% in both membrane and soluble fractions, but did not inhibit the rate of ATP-dependent phosphorylation or release of MARCKS, or decrease levels of membrane-bound PKC zeta or PKC mu. beta-12-o-tetradecanoyl-phorbol-13-acetate 38-80 myristoylated alanine rich protein kinase C substrate Homo sapiens 306-312 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). Go 6976 240-246 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9990296-6 1999 These findings support a novel mechanism by which MARCKS may be regulated by an atypical PKC isoform in phorbol ester-downregulated cells. Phorbol Esters 104-117 myristoylated alanine rich protein kinase C substrate Homo sapiens 50-56 9990296-3 1999 Pretreatment of cells with 2 microM 4 beta-12-O-tetradecanoyl-phorbol-13-acetate (beta-TPA) for 18 h downregulated conventional (PKC alpha) and novel (PKC delta) isoforms of PKC by > 90% in both membrane and soluble fractions, but did not inhibit the rate of ATP-dependent phosphorylation or release of MARCKS, or decrease levels of membrane-bound PKC zeta or PKC mu. beta-tpa 82-90 myristoylated alanine rich protein kinase C substrate Homo sapiens 306-312 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). Staurosporine 40-53 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9990296-4 1999 MARCKS phosphorylation was inhibited by staurosporine, bis-indolylmaleimide (a PKC-specific inhibitor), Go6983 (inhibits all isoforms except PKC mu), and a peptide from the calmodulin-binding domain of MARCKS, but was unaffected by EGTA or Go6976 (inhibits cPKCs and PKC mu). bisindolylmaleimide 55-75 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9808756-3 1998 To detect the activation of protein kinase C in vivo, we produced a specific antibody against MARCKS phosphorylated at serines 152 and 156. Serine 119-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 94-100 9819217-10 1998 With the IFC we show that calcium can regulate the translocation of the MARCKS effector peptide between the membrane and calmodulin (CaM) in the bulk. Calcium 26-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 10073384-2 1999 A number of studies now indicate that lithium has considerable efficacy in the prevention of suicide in patients with affective disorders, and accumulating evidence indicates that protein kinase C (PKC) and its substrates, in particular the myristoylated alanine-rich C kinase substrate (MARCKS), are primary targets of chronic lithium treatment. Lithium 328-335 myristoylated alanine rich protein kinase C substrate Homo sapiens 241-286 10073384-2 1999 A number of studies now indicate that lithium has considerable efficacy in the prevention of suicide in patients with affective disorders, and accumulating evidence indicates that protein kinase C (PKC) and its substrates, in particular the myristoylated alanine-rich C kinase substrate (MARCKS), are primary targets of chronic lithium treatment. Lithium 328-335 myristoylated alanine rich protein kinase C substrate Homo sapiens 288-294 9808756-6 1998 Phosphorylation of MARCKS was increased about eightfold by the treatment of the cells with phorbol 12-myristate 13-acetate, a protein kinase C activator. Tetradecanoylphorbol Acetate 91-122 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 9601059-2 1998 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. Phosphatidylcholines 41-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 9724518-9 1998 However, with a MARCKS peptide substrate, which formed domains of equal enrichment with L-PS and D-PS, the maximal activity of protein kinase C was the same with D-PS and with L-PS. zwittergent 3-12 97-101 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-22 9724518-9 1998 However, with a MARCKS peptide substrate, which formed domains of equal enrichment with L-PS and D-PS, the maximal activity of protein kinase C was the same with D-PS and with L-PS. zwittergent 3-12 162-166 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-22 9679146-3 1998 This report presents the first evidence that phosphorylation of the MARCKS-related domain modifies in vitro and in vivo activities of adducin involving actin and spectrin, and we demonstrate that adducin is a prominent in vivo substrate for PKC or other phorbol 12-myristate 13-acetate (PMA)-activated kinases in multiple cell types, including neurons. Tetradecanoylphorbol Acetate 254-285 myristoylated alanine rich protein kinase C substrate Homo sapiens 68-74 9679146-3 1998 This report presents the first evidence that phosphorylation of the MARCKS-related domain modifies in vitro and in vivo activities of adducin involving actin and spectrin, and we demonstrate that adducin is a prominent in vivo substrate for PKC or other phorbol 12-myristate 13-acetate (PMA)-activated kinases in multiple cell types, including neurons. Tetradecanoylphorbol Acetate 287-290 myristoylated alanine rich protein kinase C substrate Homo sapiens 68-74 9679146-5 1998 A polyclonal antibody specific to the phosphorylated state of the RTPS-serine, which is the major PKC phosphorylation site in the MARCKS-related domain, was used to evaluate phosphorylation of adducin in cells. Serine 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 9660875-12 1998 Incubation of neurons with PKCbeta subtype specific antisense oligonucleotide (AON) significantly attenuated both redistribution and phosphorylation of MARCKS. Oligonucleotides 62-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 152-158 9660875-12 1998 Incubation of neurons with PKCbeta subtype specific antisense oligonucleotide (AON) significantly attenuated both redistribution and phosphorylation of MARCKS. Oligonucleotides, Antisense 79-82 myristoylated alanine rich protein kinase C substrate Homo sapiens 152-158 9660875-13 1998 Furthermore, depletion of MARCKS by MARCKS-AON treatment of neurons resulted in a significant decrease in Ang II-stimulated accumulation of TH and DbetaH immunoreactivities and [3H]NE uptake activity in synaptosomes. Tritium 178-180 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 9660875-13 1998 Furthermore, depletion of MARCKS by MARCKS-AON treatment of neurons resulted in a significant decrease in Ang II-stimulated accumulation of TH and DbetaH immunoreactivities and [3H]NE uptake activity in synaptosomes. Tritium 178-180 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 9660875-15 1998 MARCKS pep148-165, which contains PKC phosphorylation sites, inhibited Ang II stimulation of MARCKS phosphorylation and reduced the amount of TH, DbetaH, and [3H]NE uptake in neuronal synaptosomes. Tritium 159-161 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9649335-0 1998 Poly(ADP-ribose) modulates the properties of MARCKS proteins. Poly Adenosine Diphosphate Ribose 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-51 9649335-3 1998 Here we show that poly(ADP-ribose) binds strongly to the proteins of the myristoylated alanine-rich C kinase substrate (MARCKS) family, MARCKS and MARCKS-related protein (also MacMARCKS or F52). Poly Adenosine Diphosphate Ribose 18-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 73-118 9649335-3 1998 Here we show that poly(ADP-ribose) binds strongly to the proteins of the myristoylated alanine-rich C kinase substrate (MARCKS) family, MARCKS and MARCKS-related protein (also MacMARCKS or F52). Poly Adenosine Diphosphate Ribose 18-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-126 9649335-3 1998 Here we show that poly(ADP-ribose) binds strongly to the proteins of the myristoylated alanine-rich C kinase substrate (MARCKS) family, MARCKS and MARCKS-related protein (also MacMARCKS or F52). Poly Adenosine Diphosphate Ribose 18-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 136-142 9649335-6 1998 Dot blot assays show that poly(ADP-ribose) binds to MARCKS proteins at the highly basic effector domain. Poly Adenosine Diphosphate Ribose 26-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 52-58 9649335-10 1998 Our results suggest that MARCKS proteins and actin could be targets of the poly(ADP-ribose) DNA damage signal pathway. Poly Adenosine Diphosphate Ribose 75-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 25-31 9601059-2 1998 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. Phosphatidylcholines 62-68 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 9601059-2 1998 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. Tetradecanoylphorbol Acetate 83-86 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 9601059-2 1998 Previously we showed that stimulation of phosphatidylcholine (PtdCho) synthesis by PMA in SK-N-MC human neuroblastoma cells required overexpression of MARCKS, whereas PKCalpha alone was insufficient. sk-n-mc 90-97 myristoylated alanine rich protein kinase C substrate Homo sapiens 151-157 9601059-10 1998 Our results show that MARCKS is an essential link in the PKC-mediated activation of PtdCho-specific PLD in these cells and that the stimulation of PtdCho synthesis by PMA is a secondary response. Phosphatidylcholines 84-90 myristoylated alanine rich protein kinase C substrate Homo sapiens 22-28 9536026-0 1998 Sodium valproate down-regulates the myristoylated alanine-rich C kinase substrate (MARCKS) in immortalized hippocampal cells: a property of protein kinase C-mediated mood stabilizers. Valproic Acid 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-81 9537244-7 1998 MARCKS overexpression induced a higher percentage of cells in the G0-G1 phase of the cell cycle upon serum starvation, as well as the inhibition of colony formation in soft agar. Agar 173-177 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9598313-9 1998 MACS was localized to 6q21 between D6S266 (LOD > 3.0) and AFM268uh5 by the same technique. d6s266 35-41 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 9536026-0 1998 Sodium valproate down-regulates the myristoylated alanine-rich C kinase substrate (MARCKS) in immortalized hippocampal cells: a property of protein kinase C-mediated mood stabilizers. Valproic Acid 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 83-89 9536026-4 1998 Recent studies have provided data in support of a role for protein kinase C and the down-regulation of expression of the myristoylated alanine-rich C kinase substrate (MARCKS) in the long-term therapeutic action of lithium in the brain, which is dependent on both the relative activity of receptor-coupled PI signaling and the concentration of myo-inositol. Lithium 215-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 121-166 9536026-4 1998 Recent studies have provided data in support of a role for protein kinase C and the down-regulation of expression of the myristoylated alanine-rich C kinase substrate (MARCKS) in the long-term therapeutic action of lithium in the brain, which is dependent on both the relative activity of receptor-coupled PI signaling and the concentration of myo-inositol. Lithium 215-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 168-174 9536026-4 1998 Recent studies have provided data in support of a role for protein kinase C and the down-regulation of expression of the myristoylated alanine-rich C kinase substrate (MARCKS) in the long-term therapeutic action of lithium in the brain, which is dependent on both the relative activity of receptor-coupled PI signaling and the concentration of myo-inositol. Inositol 344-356 myristoylated alanine rich protein kinase C substrate Homo sapiens 121-166 9536026-4 1998 Recent studies have provided data in support of a role for protein kinase C and the down-regulation of expression of the myristoylated alanine-rich C kinase substrate (MARCKS) in the long-term therapeutic action of lithium in the brain, which is dependent on both the relative activity of receptor-coupled PI signaling and the concentration of myo-inositol. Inositol 344-356 myristoylated alanine rich protein kinase C substrate Homo sapiens 168-174 9536026-5 1998 Our current results demonstrated that valproate induces a concentration- and time-dependent reduction of MARCKS in immortalized hippocampal cells that appears to be independent of both the level of muscarinic receptor-activated PI signaling as well as the concentration of myo-inositol. Valproic Acid 38-47 myristoylated alanine rich protein kinase C substrate Homo sapiens 105-111 9536026-5 1998 Our current results demonstrated that valproate induces a concentration- and time-dependent reduction of MARCKS in immortalized hippocampal cells that appears to be independent of both the level of muscarinic receptor-activated PI signaling as well as the concentration of myo-inositol. Inositol 273-285 myristoylated alanine rich protein kinase C substrate Homo sapiens 105-111 9536026-8 1998 Furthermore, the effect on MARCKS protein is additive in the presence of therapeutic concentrations of both lithium and valproate, consistent with clinical observations regarding the enhanced efficacy of the combination treatment. Lithium 108-115 myristoylated alanine rich protein kinase C substrate Homo sapiens 27-33 9536026-8 1998 Furthermore, the effect on MARCKS protein is additive in the presence of therapeutic concentrations of both lithium and valproate, consistent with clinical observations regarding the enhanced efficacy of the combination treatment. Valproic Acid 120-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 27-33 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phospholipids 252-265 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-182 9495248-0 1998 PMA-induced reduction in invasiveness is associated with hyperphosphorylation of MARCKS and talin in invasive bladder cancer cells. Tetradecanoylphorbol Acetate 0-3 myristoylated alanine rich protein kinase C substrate Homo sapiens 81-87 9461483-0 1998 Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes. Phospholipids 101-113 myristoylated alanine rich protein kinase C substrate Homo sapiens 11-17 9461483-0 1998 Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes. Phospholipids 101-113 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-64 9461483-12 1998 Our results show that the mechanisms regulating the interactions of MARCKS and MRP with phospholipid vesicles are, at least quantitatively, different. Phospholipids 88-100 myristoylated alanine rich protein kinase C substrate Homo sapiens 68-74 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phospholipids 252-265 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylserines 266-284 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-182 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylserines 266-284 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylserines 286-288 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-182 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylserines 286-288 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 294-331 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-182 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 294-331 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 333-337 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-182 9533686-1 1998 Direct fluorescence digital imaging microscopy observations demonstrate that a basic peptide corresponding to the effector region of the myristoylated alanine-rich C kinase substrate (MARCKS) self-assembles into membrane domains enriched in the acidic phospholipids phosphatidylserine (PS) and phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 333-337 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 9533686-2 1998 We show here that pentalysine, which corresponds to the first five residues of the MARCKS effector region peptide and binds to membranes through electrostatic interactions, also forms domains enriched in PS and PIP2. pentalysine 18-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 83-89 9674936-6 1998 Subsequent studies involving regulation of inositol transport, PKC isozymes and activity, and the expression of the major PKC substrate MARCKS (myristoylated alanine-rich C-kinase substrate) have offered potential avenues for understanding the complexity of the action of long-term lithium in the brain. Lithium 282-289 myristoylated alanine rich protein kinase C substrate Homo sapiens 136-142 9523737-7 1998 Furthermore, gemcitabine (10 microM) activated protein kinase C in BG-1 cells and the phosphorylation of the endogenous protein kinase C substrate, myristoylated alanine-rich C kinase substrate, was increased following exposure of BG-1 cells to gemcitabine for up to 6 h. Clonogenicity studies with gemcitabine in combination with various protein kinase C-modulating agents demonstrated that gemcitabine cytotoxicity was influenced by protein kinase C signaling events in BG-1 cells. gemcitabine 13-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-193 9523737-7 1998 Furthermore, gemcitabine (10 microM) activated protein kinase C in BG-1 cells and the phosphorylation of the endogenous protein kinase C substrate, myristoylated alanine-rich C kinase substrate, was increased following exposure of BG-1 cells to gemcitabine for up to 6 h. Clonogenicity studies with gemcitabine in combination with various protein kinase C-modulating agents demonstrated that gemcitabine cytotoxicity was influenced by protein kinase C signaling events in BG-1 cells. gemcitabine 245-256 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-193 9523737-7 1998 Furthermore, gemcitabine (10 microM) activated protein kinase C in BG-1 cells and the phosphorylation of the endogenous protein kinase C substrate, myristoylated alanine-rich C kinase substrate, was increased following exposure of BG-1 cells to gemcitabine for up to 6 h. Clonogenicity studies with gemcitabine in combination with various protein kinase C-modulating agents demonstrated that gemcitabine cytotoxicity was influenced by protein kinase C signaling events in BG-1 cells. gemcitabine 245-256 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-193 9523737-7 1998 Furthermore, gemcitabine (10 microM) activated protein kinase C in BG-1 cells and the phosphorylation of the endogenous protein kinase C substrate, myristoylated alanine-rich C kinase substrate, was increased following exposure of BG-1 cells to gemcitabine for up to 6 h. Clonogenicity studies with gemcitabine in combination with various protein kinase C-modulating agents demonstrated that gemcitabine cytotoxicity was influenced by protein kinase C signaling events in BG-1 cells. gemcitabine 245-256 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-193 9674936-6 1998 Subsequent studies involving regulation of inositol transport, PKC isozymes and activity, and the expression of the major PKC substrate MARCKS (myristoylated alanine-rich C-kinase substrate) have offered potential avenues for understanding the complexity of the action of long-term lithium in the brain. Lithium 282-289 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-189 9341159-2 1997 Previous studies with a peptide corresponding to the effector region, MARCKS-(151-175), showed that the 13 basic residues interact electrostatically with acidic lipids and that the 5 hydrophobic phenylalanine residues penetrate the polar head group region of the bilayer. Phenylalanine 195-208 myristoylated alanine rich protein kinase C substrate Homo sapiens 70-76 9341159-10 1997 We discuss the biological implications of this switch mechanism, speculating that an increase in the level of Ca2+-calmodulin could rapidly release phosphatidylinositol 4, 5-bisphosphate that previous work has suggested is sequestered in lateral domains formed by MARCKS and MARCKS-(151-175). Phosphatidylinositol 4,5-Diphosphate 148-186 myristoylated alanine rich protein kinase C substrate Homo sapiens 264-270 9341159-10 1997 We discuss the biological implications of this switch mechanism, speculating that an increase in the level of Ca2+-calmodulin could rapidly release phosphatidylinositol 4, 5-bisphosphate that previous work has suggested is sequestered in lateral domains formed by MARCKS and MARCKS-(151-175). Phosphatidylinositol 4,5-Diphosphate 148-186 myristoylated alanine rich protein kinase C substrate Homo sapiens 275-281 9295331-6 1997 Here we show that p40, the carboxyl-terminal fragment resulting from this cleavage of MARCKS, was associated with the mitochondrial/lysosomal pellet fraction of human diploid fibroblasts and that its generation in cells was sensitive to treatment with NH4Cl. Ammonium Chloride 252-257 myristoylated alanine rich protein kinase C substrate Homo sapiens 86-92 9259558-5 1997 While at the membrane, MARCKS binds to and sequesters acidic phospholipids including phosphatidyl-inositol-4,5-bisphosphate (PIP2) [7]. Phospholipids 61-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-29 9259558-5 1997 While at the membrane, MARCKS binds to and sequesters acidic phospholipids including phosphatidyl-inositol-4,5-bisphosphate (PIP2) [7]. Phosphatidylinositol 4,5-Diphosphate 85-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-29 9259558-5 1997 While at the membrane, MARCKS binds to and sequesters acidic phospholipids including phosphatidyl-inositol-4,5-bisphosphate (PIP2) [7]. Phosphatidylinositol 4,5-Diphosphate 125-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-29 9259558-10 1997 Our results provide direct evidence that MARCKS and PKC regulate actin-dependent membrane ruffling and cell adhesion, perhaps via a PIP2-dependent mechanism. Phosphatidylinositol 4,5-Diphosphate 132-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-47 9483901-2 1997 Zn and Cu content of the soil exceeds the background levels and approaches the MACs. Zinc 0-2 myristoylated alanine rich protein kinase C substrate Homo sapiens 79-83 9150270-1 1997 MARCKS (myristoylated alanine-rich C-kinase substrate) is known to interact with calmodulin, actin filaments, and anionic phospholipids at a central basic domain which is also the site of phosphorylation by protein kinase C (PKC). Phospholipids 122-135 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 9150270-1 1997 MARCKS (myristoylated alanine-rich C-kinase substrate) is known to interact with calmodulin, actin filaments, and anionic phospholipids at a central basic domain which is also the site of phosphorylation by protein kinase C (PKC). Phospholipids 122-135 myristoylated alanine rich protein kinase C substrate Homo sapiens 8-53 9150270-3 1997 CD treatment for 1 h disrupted F-actin filaments, increased membrane bound immunoreactive MARCKS (from 51% to 62% of total), yet markedly enhanced the amount of MARCKS translocated to the cytosolic fraction in response to the phorbol ester 4beta-12-O-tetradecanoylphorbol 13-acetate. Cytochalasin D 0-2 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 9150270-3 1997 CD treatment for 1 h disrupted F-actin filaments, increased membrane bound immunoreactive MARCKS (from 51% to 62% of total), yet markedly enhanced the amount of MARCKS translocated to the cytosolic fraction in response to the phorbol ester 4beta-12-O-tetradecanoylphorbol 13-acetate. Cytochalasin D 0-2 myristoylated alanine rich protein kinase C substrate Homo sapiens 161-167 9150270-3 1997 CD treatment for 1 h disrupted F-actin filaments, increased membrane bound immunoreactive MARCKS (from 51% to 62% of total), yet markedly enhanced the amount of MARCKS translocated to the cytosolic fraction in response to the phorbol ester 4beta-12-O-tetradecanoylphorbol 13-acetate. Phorbol Esters 226-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 161-167 9150270-3 1997 CD treatment for 1 h disrupted F-actin filaments, increased membrane bound immunoreactive MARCKS (from 51% to 62% of total), yet markedly enhanced the amount of MARCKS translocated to the cytosolic fraction in response to the phorbol ester 4beta-12-O-tetradecanoylphorbol 13-acetate. 4beta-12-o-tetradecanoylphorbol 13-acetate 240-282 myristoylated alanine rich protein kinase C substrate Homo sapiens 161-167 9040691-6 1997 PKC activation was determined by measurement of myristoylated, alanine-rich C kinase substrate (MARCKS) phosphorylation in digitonin-permeabilized VSMCs. Digitonin 123-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-94 9040691-6 1997 PKC activation was determined by measurement of myristoylated, alanine-rich C kinase substrate (MARCKS) phosphorylation in digitonin-permeabilized VSMCs. Digitonin 123-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 9040691-6 1997 PKC activation was determined by measurement of myristoylated, alanine-rich C kinase substrate (MARCKS) phosphorylation in digitonin-permeabilized VSMCs. vsmcs 147-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-94 9040691-6 1997 PKC activation was determined by measurement of myristoylated, alanine-rich C kinase substrate (MARCKS) phosphorylation in digitonin-permeabilized VSMCs. vsmcs 147-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 9112755-0 1997 Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP). Calcium 0-7 myristoylated alanine rich protein kinase C substrate Homo sapiens 97-142 9112755-0 1997 Calcium binding and conformational properties of calmodulin complexed with peptides derived from myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP). Calcium 0-7 myristoylated alanine rich protein kinase C substrate Homo sapiens 144-150 8978751-5 1997 Subcellular fractionation studies also showed that the myristoylated alanine-rich C-kinase substrate (MARCKS), a major neuronal PKC substrate that has been implicated in the mechanism of neurotransmitter release, translocated from membranes to cytosol in response to an 8-min TPA treatment. Tetradecanoylphorbol Acetate 276-279 myristoylated alanine rich protein kinase C substrate Homo sapiens 102-108 8978751-7 1997 The ability of TPA to enhance NA release and to cause the translocation and phosphorylation of MARCKS was inhibited by the PKC inhibitor Ro 31-8220 (10 microM). Tetradecanoylphorbol Acetate 15-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 95-101 8978751-7 1997 The ability of TPA to enhance NA release and to cause the translocation and phosphorylation of MARCKS was inhibited by the PKC inhibitor Ro 31-8220 (10 microM). Ro 31-8220 137-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 95-101 8978751-8 1997 Selective down-regulation of PKC subtypes by prolonged exposure to phorbol 12,13-dibutyrate (100 nM) attenuated the TPA-induced enhancement of NA release and the translocation of MARCKS over an interval similar to that of down-regulation of PKC-alpha (but not -epsilon or -zeta). Phorbol 12,13-Dibutyrate 67-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 179-185 9150270-5 1997 Staurosporine also increased membrane association of MARCKS in a PKC-independent manner, as no change in MARCKS phosphorylation was noted and bis-indolylmaleimide (a more specific PKC inhibitor) did not alter MARCKS distribution. Staurosporine 0-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 9150270-6 1997 Staurosporine inhibited the phorbol ester-induced translocation of MARCKS but not of PKC alpha in both CD pretreated and untreated cells. Staurosporine 0-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 67-73 9150270-6 1997 Staurosporine inhibited the phorbol ester-induced translocation of MARCKS but not of PKC alpha in both CD pretreated and untreated cells. Phorbol Esters 28-41 myristoylated alanine rich protein kinase C substrate Homo sapiens 67-73 9150270-6 1997 Staurosporine inhibited the phorbol ester-induced translocation of MARCKS but not of PKC alpha in both CD pretreated and untreated cells. Cytochalasin D 103-105 myristoylated alanine rich protein kinase C substrate Homo sapiens 67-73 9150270-7 1997 Calmodulin antagonists (trifluoperazine, calmidazolium) had little effect on the cellular distribution or phosphorylation of MARCKS, but were synergistic with phorbol ester in translocating MARCKS from the membrane without a further increase in its phosphorylation. Trifluoperazine 24-39 myristoylated alanine rich protein kinase C substrate Homo sapiens 190-196 9150270-7 1997 Calmodulin antagonists (trifluoperazine, calmidazolium) had little effect on the cellular distribution or phosphorylation of MARCKS, but were synergistic with phorbol ester in translocating MARCKS from the membrane without a further increase in its phosphorylation. calmidazolium 41-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 190-196 9150270-7 1997 Calmodulin antagonists (trifluoperazine, calmidazolium) had little effect on the cellular distribution or phosphorylation of MARCKS, but were synergistic with phorbol ester in translocating MARCKS from the membrane without a further increase in its phosphorylation. Phorbol Esters 159-172 myristoylated alanine rich protein kinase C substrate Homo sapiens 190-196 9112755-4 1997 The wild-type MARCKS and MRP peptides induced significant increases in the Ca2+ affinity of CaM (pCa 6.1 and 5.8, respectively, compared to 5.2, for CaM in the absence of bound peptides), whereas a modified MARCKS peptide, in which the four serine residues susceptible to phosphorylation in the wild-type sequence have been replaced with aspartate residues to mimic phosphorylation, had smaller effect (pCa 5.6). Serine 241-247 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 9112755-4 1997 The wild-type MARCKS and MRP peptides induced significant increases in the Ca2+ affinity of CaM (pCa 6.1 and 5.8, respectively, compared to 5.2, for CaM in the absence of bound peptides), whereas a modified MARCKS peptide, in which the four serine residues susceptible to phosphorylation in the wild-type sequence have been replaced with aspartate residues to mimic phosphorylation, had smaller effect (pCa 5.6). Aspartic Acid 338-347 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 8978751-8 1997 Selective down-regulation of PKC subtypes by prolonged exposure to phorbol 12,13-dibutyrate (100 nM) attenuated the TPA-induced enhancement of NA release and the translocation of MARCKS over an interval similar to that of down-regulation of PKC-alpha (but not -epsilon or -zeta). Tetradecanoylphorbol Acetate 116-119 myristoylated alanine rich protein kinase C substrate Homo sapiens 179-185 8978751-9 1997 Thus, we have demonstrated a strong correlation between the translocation of MARCKS and the enhancement of NA release from SH-SY5Y cells due to the TPA-induced activation of PKC-alpha. Tetradecanoylphorbol Acetate 148-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 77-83 9483901-2 1997 Zn and Cu content of the soil exceeds the background levels and approaches the MACs. Copper 7-9 myristoylated alanine rich protein kinase C substrate Homo sapiens 79-83 8906563-2 1996 Correlation with metabolism of membrane phospholipids suggests that PKC-alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester (beta-TPA). Phospholipids 40-53 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 8824266-0 1996 Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. Phosphatidylinositol 4,5-Diphosphate 121-158 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 8824266-0 1996 Myristoylated alanine-rich C kinase substrate (MARCKS) produces reversible inhibition of phospholipase C by sequestering phosphatidylinositol 4,5-bisphosphate in lateral domains. Phosphatidylinositol 4,5-Diphosphate 121-158 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 8824266-4 1996 The present study shows that physiological concentrations of MARCKS (<10 microM) inhibit phospholipase C (PLC)-catalyzed hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) in phospholipid vesicles. Phosphatidylinositol 4,5-Diphosphate 138-175 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 8824266-4 1996 The present study shows that physiological concentrations of MARCKS (<10 microM) inhibit phospholipase C (PLC)-catalyzed hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) in phospholipid vesicles. Phosphatidylinositol 4,5-Diphosphate 177-181 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 8824266-4 1996 The present study shows that physiological concentrations of MARCKS (<10 microM) inhibit phospholipase C (PLC)-catalyzed hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) in phospholipid vesicles. Phospholipids 186-198 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 8824266-6 1996 Direct fluorescence microscopy observations demonstrate that the MARCKS peptide forms lateral domains enriched in the acidic lipids phosphatidylserine and PIP2 but not PLC, which accounts for the observed inhibition of PIP2 hydrolysis. Phosphatidylinositol 4,5-Diphosphate 155-159 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 8824266-7 1996 Phosphorylation of MARCKS(151-175) by PKC releases the inhibition and allows PLC to produce a burst of inositol 1,4, 5-trisphosphate and diacylglycerol. Inositol 1,4,5-Trisphosphate 103-132 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 8824266-7 1996 Phosphorylation of MARCKS(151-175) by PKC releases the inhibition and allows PLC to produce a burst of inositol 1,4, 5-trisphosphate and diacylglycerol. Diglycerides 137-151 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 8858924-6 1996 Protein kinase C (PKC)-dependent phosphorylation of two proteins identified as GAP-43 and MARCKS protein was enhanced in the intact IGC stimulated by GABA, resulting in the release of MARCKS protein and GAP-43 from the membrane. gamma-Aminobutyric Acid 150-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 8858924-6 1996 Protein kinase C (PKC)-dependent phosphorylation of two proteins identified as GAP-43 and MARCKS protein was enhanced in the intact IGC stimulated by GABA, resulting in the release of MARCKS protein and GAP-43 from the membrane. gamma-Aminobutyric Acid 150-154 myristoylated alanine rich protein kinase C substrate Homo sapiens 184-190 8906563-2 1996 Correlation with metabolism of membrane phospholipids suggests that PKC-alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester (beta-TPA). Phosphatidylcholines 116-135 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 8906563-2 1996 Correlation with metabolism of membrane phospholipids suggests that PKC-alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester (beta-TPA). Phorbol Esters 159-172 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 8906563-2 1996 Correlation with metabolism of membrane phospholipids suggests that PKC-alpha and MARCKS may be required to mediate phosphatidylcholine turnover stimulated by phorbol ester (beta-TPA). beta-tpa 174-182 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 8906563-8 1996 Thus, induced differentiation of human neuroblastoma cells involved increased expression of PKC-alpha and MARCKS and synthesis of phosphatidylcholine, consistent with involvement of PKC-alpha and MARCKS in regulation of phosphatidylcholine turnover during neurite growth. Phosphatidylcholines 220-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 196-202 8842533-11 1996 Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC-beta 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginic-rich C kinase substrate (MARCKS) phosphorylation. Phorbol Esters 18-31 myristoylated alanine rich protein kinase C substrate Homo sapiens 170-215 8702537-7 1996 Mutation of the N-terminal glycine results in a nonmyristoylated form of MARCKS which does not bind membranes and is poorly phosphorylated. Glycine 27-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 73-79 8702537-8 1996 This indicates that myristic acid targets MARCKS to the membrane, where it is efficiently phosphorylated by PKC. Myristic Acid 20-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 42-48 8702537-13 1996 In addition to the nonspecific membrane binding interactions conferred by the myristoyl-electrostatic switch, indirect immunofluorescence microscopy demonstrates that specific protein-protein interactions also specify the intracellular localization of MARCKS. myristoyl 78-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 252-258 8842533-11 1996 Moreover, chronic phorbol ester treatment induced an 84,000 Mr PKC-beta 2 isoform that appeared to be persistently translocated and activated, as suggested by studies of myristoylated arginic-rich C kinase substrate (MARCKS) phosphorylation. Phorbol Esters 18-31 myristoylated alanine rich protein kinase C substrate Homo sapiens 217-223 8627336-0 1996 Overexpression of MARCKS, but not protein kinase C-alpha, increases phorbol ester-stimulated synthesis of phosphatidylcholine in human SK-N-MC neuroblastoma cells. Phorbol Esters 68-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 8627336-0 1996 Overexpression of MARCKS, but not protein kinase C-alpha, increases phorbol ester-stimulated synthesis of phosphatidylcholine in human SK-N-MC neuroblastoma cells. Phosphatidylcholines 106-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 8627336-1 1996 To investigate the regulation of phorbol ester-stimulated synthesis of phosphatidylcholine (PtdCho), myristoylated alanine-rich protein kinase C substrate (MARCKS) and the alpha-isoform of protein kinase C (PKC-alpha) were overexpressed in a human neuroblastoma (SK-N-MC) cell line that does not increase PtdCho synthesis in response to 4beta-12-O-tetradecanoylphorbol 13-acetate (TPA). Phorbol Esters 33-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 101-154 8627336-2 1996 In five clones with a less than fivefold increase in MARCKS protein level, the synthesis of PtdCho from [methyl-3H] choline was stimulated 1.88-2.34-fold in the presence of 100-200 nM TPA. Phosphatidylcholines 92-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 8627336-2 1996 In five clones with a less than fivefold increase in MARCKS protein level, the synthesis of PtdCho from [methyl-3H] choline was stimulated 1.88-2.34-fold in the presence of 100-200 nM TPA. [methyl-3h] choline 104-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. sulfhydryl reactive proxyl nitroxide 203-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-153 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. sulfhydryl reactive proxyl nitroxide 203-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 155-161 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. Cysteine 0-8 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-153 8769854-7 1996 The inactivation of PKC activity was confirmed by the fact that phosphorylation of the MARCKS protein, a PKC-selective substrate, was reduced in intact neurons following transient glutamate treatment. Glutamic Acid 180-189 myristoylated alanine rich protein kinase C substrate Homo sapiens 87-93 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. Cysteine 0-8 myristoylated alanine rich protein kinase C substrate Homo sapiens 155-161 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. Peptides 21-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-153 8608129-1 1996 Cysteine-substituted peptides based on the membrane, calmodulin, and protein kinase C binding domain of the myristoylated alanine rich C kinase substrate (MARCKS) were synthesized and derivatized with a sulfhydryl reactive proxyl nitroxide. Peptides 21-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 155-161 8601451-6 1996 However, in contrast to other PKCs, a peptide derived from the MARCKS phosphorylation domain is phosphorylated only at serine 156, and not at serines 152 and 163, implicating a differential regulation by PKC mu. Serine 119-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 63-69 8596017-2 1996 Incubation of B-chronic lymphocytic leukemia (B-CLL) cells with phorbol esters resulted in the phosphorylation of two major PKC substrates, MARCKS (myristoylated, alanine-rich C kinase substrate) and MRP (MARCKS-related protein), and of a third protein, with an apparent m.w. Phorbol Esters 64-78 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-146 8602119-0 1996 Ethanol enhances the in situ phosphorylation of MARCKS and protein kinase C activity in primary cultures of astrocytes. Ethanol 0-7 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 57-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 8611023-0 1996 Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C. The myristoylated aline-rich protein kinase C substrate (MARCKS) is a peripheral membrane protein that undergoes phosphorylation-dependent translocation between membrane and cytosol. Phosphatidylinositols 68-85 myristoylated alanine rich protein kinase C substrate Homo sapiens 142-193 8611023-0 1996 Binding of myristoylated alanine-rich protein kinase C substrate to phosphoinositides attenuates the phosphorylation by protein kinase C. The myristoylated aline-rich protein kinase C substrate (MARCKS) is a peripheral membrane protein that undergoes phosphorylation-dependent translocation between membrane and cytosol. Phosphatidylinositols 68-85 myristoylated alanine rich protein kinase C substrate Homo sapiens 195-201 8611023-1 1996 MARCKS binds to acidic phospholipids with high affinity (Kd less than 0.5 microM) but binds poorly to neutral phospholipids. Phospholipids 23-36 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8611023-1 1996 MARCKS binds to acidic phospholipids with high affinity (Kd less than 0.5 microM) but binds poorly to neutral phospholipids. Phospholipids 110-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8611023-2 1996 Although interaction of MARCKS with acidic phospholipids lacks specificity when determined by binding assay, these phospholipids exert distinctive effects on the phosphorylation of this protein by protein kinase C (PKC). Phospholipids 43-56 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-30 8611023-2 1996 Although interaction of MARCKS with acidic phospholipids lacks specificity when determined by binding assay, these phospholipids exert distinctive effects on the phosphorylation of this protein by protein kinase C (PKC). Phospholipids 115-128 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-30 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidylserines 29-47 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidylserines 49-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidylglycerols 56-76 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidic Acids 120-137 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidylinositols 139-159 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. phosphatidylinositol 4-phosphate 166-198 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-3 1996 Preincubation of MARCKS with phosphatidylserine (PS) or phosphatidylglycerol enhanced the phosphorylation; whereas with phosphatidic acid, phosphatidylinositol (PI), phosphatidylinositol-4-phosphate, or phosphatidylinositol-4,5-biphosphate inhibited the phosphorylation of this substrate by PKC. Phosphatidylinositol 4,5-Diphosphate 203-239 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 8611023-4 1996 Phosphoinositide inhibition of MARCKS phosphorylation was apparently directed at the substrate rather than at the kinase as the phosphorylation of two other phospholipid-binding PKC substrates, neuromodulin and neurogranin, exhibited different responses from those of MARCKS. Phosphatidylinositols 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 31-37 8611023-4 1996 Phosphoinositide inhibition of MARCKS phosphorylation was apparently directed at the substrate rather than at the kinase as the phosphorylation of two other phospholipid-binding PKC substrates, neuromodulin and neurogranin, exhibited different responses from those of MARCKS. Phosphatidylinositols 0-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 268-274 8611023-4 1996 Phosphoinositide inhibition of MARCKS phosphorylation was apparently directed at the substrate rather than at the kinase as the phosphorylation of two other phospholipid-binding PKC substrates, neuromodulin and neurogranin, exhibited different responses from those of MARCKS. Phospholipids 157-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 31-37 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phosphatidylinositols 27-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phosphatidylinositols 27-44 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-143 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phosphatidylserines 49-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phosphatidylserines 49-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-143 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phospholipids 124-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 8611023-7 1996 These results suggest that phosphoinositides and PS bind at different residues within the MARCKS PSD, so that the resulting phospholipid/MARCKS complexes are differentially phosphorylated by PKC. Phospholipids 124-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 137-143 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 45-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 8557118-0 1996 PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. Serine 57-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 8602119-4 1996 Chronic ethanol exposure also increased the in situ phosphorylation of MARCKS in permeabilized astrocytes both in the absence or presence of the PKC activator, phorbol 12 -myristate 13 -acetate (PMA). Ethanol 8-15 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 8602119-4 1996 Chronic ethanol exposure also increased the in situ phosphorylation of MARCKS in permeabilized astrocytes both in the absence or presence of the PKC activator, phorbol 12 -myristate 13 -acetate (PMA). Tetradecanoylphorbol Acetate 160-193 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 8602119-4 1996 Chronic ethanol exposure also increased the in situ phosphorylation of MARCKS in permeabilized astrocytes both in the absence or presence of the PKC activator, phorbol 12 -myristate 13 -acetate (PMA). Tetradecanoylphorbol Acetate 195-198 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 8834063-5 1996 In most cases, stimulation of cells with a phorbol ester led to a slight increase (20-30%) in MARCKS phosphorylation. Phorbol Esters 43-56 myristoylated alanine rich protein kinase C substrate Homo sapiens 94-100 7889145-7 1995 To assess the effects of H2O2 treatment on PKC activation, we measured phosphorylation of an endogenous PKC substrate, the MARCKS (myristoylated alanine-rich C kinase substrate) protein. Hydrogen Peroxide 25-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 131-176 8519597-0 1995 Phosphorylation of MARCKS, neuromodulin, and neurogranin by protein kinase C exhibits differential responses to diacylglycerols. Diglycerides 112-127 myristoylated alanine rich protein kinase C substrate Homo sapiens 19-25 8519597-1 1995 Diacylglycerols (DG) derived from brain phosphatidylinositol (PI) and phosphatidylcholine (PC) and synthetic 1,2-dioleoylglycerol (diC18:1) and 1,2-dioctanoylglycerol (diC8) were tested for their efficacy in stimulating PKC-catalyzed phosphorylation of three physiological substrates in the brain, namely, MARCKS, neuromodulin (Nm), and neurogranin (Ng). Diglycerides 0-15 myristoylated alanine rich protein kinase C substrate Homo sapiens 306-312 7603834-0 1995 Cholecystokinin-octapeptide affects the fluorescence signal of a single pancreatic acinar cell loaded with the acrylodan-labelled MARCKS peptide, a protein kinase C substrate. acrylodan 111-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 7603834-2 1995 The diffusion of the acrylodan-labelled MARCKS-peptide into the cell interior could be monitored by the increase of fluorescence in the whole-cell patch-clamp configuration. acrylodan 21-30 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 7840634-7 1995 CaM and S100 inhibited the PKM-catalyzed phosphorylation of MARCKS only in the presence of Ca2+ and addition of phosphatidylserine (PS)/dioleoylglycerol (DG) did not influence the inhibitory effect. Phosphatidylserines 112-130 myristoylated alanine rich protein kinase C substrate Homo sapiens 60-66 7840634-7 1995 CaM and S100 inhibited the PKM-catalyzed phosphorylation of MARCKS only in the presence of Ca2+ and addition of phosphatidylserine (PS)/dioleoylglycerol (DG) did not influence the inhibitory effect. Phosphatidylserines 132-134 myristoylated alanine rich protein kinase C substrate Homo sapiens 60-66 7840634-7 1995 CaM and S100 inhibited the PKM-catalyzed phosphorylation of MARCKS only in the presence of Ca2+ and addition of phosphatidylserine (PS)/dioleoylglycerol (DG) did not influence the inhibitory effect. diolein 136-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 60-66 7796455-3 1995 Similarly, alterations in polyphosphoinositide metabolism that occur in transformed cells may also promote or induce alterations in the microfilament cytoskeleton via interactions with proteins such as gelsolin, alpha-actinin, and MARCKS [Bretscher, 1993]. Phosphatidylinositol Phosphates 26-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 231-237 9064101-4 1996 The results formed basis for sanitary measures, establishment of MACs for 4 monocrystalline compounds in the air of workplace. monocrystalline 76-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-69 7650489-7 1995 Phagocytosis of zymosan was accompanied by rapid and sustained phosphorylation of MARCKS. Zymosan 16-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 7667880-2 1995 The myristoylated alanine-rich C kinase substrate (MARCKS), Src, ADP-ribosylation factor and human immunodeficiency virus-1 matrix proteins also contain a cluster of basic residues that bind to acidic phospholipids; the hydrophobic and electrostatic interactions act together to anchor the protein to a membrane. Phospholipids 201-214 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 7667880-3 1995 For MARCKS, and perhaps other proteins, phosphorylation of serines within its basic cluster reduces the electrostatic attraction, producing translocation of the protein from the membrane to the cytosol by a simple "electrostatic switch" mechanism. Serine 59-66 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-10 7720702-6 1995 MARCKS phosphorylation is required for its translocation to lysosomes since mutating either the serine residues phosphorylated by PKC (phos-) or the PKC inhibitor staurosporine, prevented MARCKS phosphorylation, its release from the plasma membrane, and its subsequent association with lysosomes. Serine 96-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 7720702-6 1995 MARCKS phosphorylation is required for its translocation to lysosomes since mutating either the serine residues phosphorylated by PKC (phos-) or the PKC inhibitor staurosporine, prevented MARCKS phosphorylation, its release from the plasma membrane, and its subsequent association with lysosomes. Serine 96-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-194 7720702-6 1995 MARCKS phosphorylation is required for its translocation to lysosomes since mutating either the serine residues phosphorylated by PKC (phos-) or the PKC inhibitor staurosporine, prevented MARCKS phosphorylation, its release from the plasma membrane, and its subsequent association with lysosomes. Staurosporine 163-176 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 7720702-7 1995 In the presence of lysosomotropic agents or nocodazole, MARCKS accumulated on lysosomes and returned to the plasma membrane upon drug removal, further suggesting that the protein cycles between the plasma membrane and lysosomes. Nocodazole 44-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 7531492-4 1995 The degree of enrichment of the MARCKS peptide in the phosphatidylserine domains decreased proportionally with protein kinase C activity when polylysine was added. Polylysine 142-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 32-38 7531492-5 1995 Polylysine caused the MARCKS peptide to be displaced from the domains into the nondomain areas of the vesicles. Polylysine 0-10 myristoylated alanine rich protein kinase C substrate Homo sapiens 22-28 7744285-1 1995 The study of general toxicological mechanism of acetone cyanhydrin and cyanides provided the data for reconsideration of their MACs in the water which is recommended at the level of 0.035 mg/l (as CN for each substance alone and both together). acetone cyanohydrin 48-66 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-131 7889145-8 1995 Treatment of cells with 0.2-1.0 mM H2O2 resulted in a rapid increase in MARCKS phosphorylation. Hydrogen Peroxide 35-39 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 7744285-1 1995 The study of general toxicological mechanism of acetone cyanhydrin and cyanides provided the data for reconsideration of their MACs in the water which is recommended at the level of 0.035 mg/l (as CN for each substance alone and both together). Cyanides 71-79 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-131 7744285-1 1995 The study of general toxicological mechanism of acetone cyanhydrin and cyanides provided the data for reconsideration of their MACs in the water which is recommended at the level of 0.035 mg/l (as CN for each substance alone and both together). Water 139-144 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-131 7889145-10 1995 Treatment with phorbol 12-myristate 13-acetate, a PKC activator, increased MARCKS phosphorylation approximately 4-fold. Tetradecanoylphorbol Acetate 15-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-81 7889145-11 1995 The H2O2-induced MARCKS phosphorylation was inhibited by the addition of the kinase inhibitors H-7 and staurosporine. Hydrogen Peroxide 4-8 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 7889145-11 1995 The H2O2-induced MARCKS phosphorylation was inhibited by the addition of the kinase inhibitors H-7 and staurosporine. 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine 95-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 7889145-11 1995 The H2O2-induced MARCKS phosphorylation was inhibited by the addition of the kinase inhibitors H-7 and staurosporine. Staurosporine 103-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 7889145-12 1995 Furthermore, specific down-regulation of PKC by phorbol ester also inhibited H2O2-induced MARCKS phosphorylation. Phorbol Esters 48-61 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 7889145-12 1995 Furthermore, specific down-regulation of PKC by phorbol ester also inhibited H2O2-induced MARCKS phosphorylation. Hydrogen Peroxide 77-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 90-96 7767386-1 1995 Several proteins that are important components of the calcium/phospholipid second messenger system (e.g. phospholipase C, protein kinase C, myristoylated alanine-rich C kinase substrate (MARCKS) and pp60src) contain clusters of basic residues that can interact with acidic lipids on the cytoplasmic surface of plasma membranes. Calcium 54-61 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-185 7767386-1 1995 Several proteins that are important components of the calcium/phospholipid second messenger system (e.g. phospholipase C, protein kinase C, myristoylated alanine-rich C kinase substrate (MARCKS) and pp60src) contain clusters of basic residues that can interact with acidic lipids on the cytoplasmic surface of plasma membranes. Phospholipids 62-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-185 7964753-7 1994 Addition of beta-12-O-tetradecanoylphorbol 13-acetate resulted in three- to fourfold increased phosphorylation of MARCKS in HTB-11 cells, with little increase noted in HTB-10 cells. beta-12-o-tetradecanoylphorbol 13-acetate 12-53 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-120 8524738-4 1995 For contents of benz(a)pyrene and mineral oils exceeding 2.5 to 3.5 times the respective occupational environment MACs, evidence from cytogenetic analysis showed substantial, 4-fold, increase in indexes of genotoxic impairment (frequency of micronucleated-binucleated lymphocytes, number of micronuclei per 1000 binucleated lymphocytes) in the workers investigated. Benzo(a)pyrene 16-29 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-118 8524738-4 1995 For contents of benz(a)pyrene and mineral oils exceeding 2.5 to 3.5 times the respective occupational environment MACs, evidence from cytogenetic analysis showed substantial, 4-fold, increase in indexes of genotoxic impairment (frequency of micronucleated-binucleated lymphocytes, number of micronuclei per 1000 binucleated lymphocytes) in the workers investigated. Mineral Oil 34-46 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-118 7964753-9 1994 Of these proteins, only MARCKS appears to be correlated with phorbol ester stimulation of phosphatidylcholine turnover in these cells. Phorbol Esters 61-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-30 7964753-9 1994 Of these proteins, only MARCKS appears to be correlated with phorbol ester stimulation of phosphatidylcholine turnover in these cells. Phosphatidylcholines 90-109 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-30 7931322-0 1994 Phorbol ester- and retinoic acid-induced regulation of the protein kinase C substrate MARCKS in immortalized hippocampal cells. Phorbol Esters 0-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 86-92 7931322-0 1994 Phorbol ester- and retinoic acid-induced regulation of the protein kinase C substrate MARCKS in immortalized hippocampal cells. Tretinoin 19-32 myristoylated alanine rich protein kinase C substrate Homo sapiens 86-92 7931322-1 1994 The expression of MARCKS, a major protein kinase C (PKC) substrate, was examined in the immortalized hippocampal cell line HN33, following differentiation using phorbol esters or retinoic acid. Phorbol Esters 161-175 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 7931322-1 1994 The expression of MARCKS, a major protein kinase C (PKC) substrate, was examined in the immortalized hippocampal cell line HN33, following differentiation using phorbol esters or retinoic acid. Tretinoin 179-192 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 7931322-2 1994 In cells exposed to phorbol esters, MARCKS protein levels were reduced through an apparent PKC-dependent mechanism. Phorbol Esters 20-34 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 7931322-6 1994 The reduction in MARCKS protein levels was maximal following 24 h of PMA exposure. Tetradecanoylphorbol Acetate 69-72 myristoylated alanine rich protein kinase C substrate Homo sapiens 17-23 7931322-7 1994 MARCKS protein expression was also down-regulated in a dose-dependent manner on exposure of HN33 cells to retinoic acid. Tretinoin 106-119 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 7931322-8 1994 In cells exposed to 10 microM retinoic acid, the MARCKS protein level was reduced in the membrane fraction within 4 h. Reduction of MARCKS protein levels was maximal (> 90%) by 12 h with no evidence for any alteration in PKC activity. Tretinoin 30-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 7931322-8 1994 In cells exposed to 10 microM retinoic acid, the MARCKS protein level was reduced in the membrane fraction within 4 h. Reduction of MARCKS protein levels was maximal (> 90%) by 12 h with no evidence for any alteration in PKC activity. Tretinoin 30-43 myristoylated alanine rich protein kinase C substrate Homo sapiens 132-138 7931322-9 1994 Reduced levels of MARCKS protein were also observed in the soluble fraction of retinoic acid-exposed cells, but to a significantly lesser extent. Tretinoin 79-92 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 7931322-10 1994 Addition of the PKC inhibitor GF109203X blocked the down-regulation of MARCKS protein in PMA-treated cultures but not in retinoic acid-treated cells. bisindolylmaleimide I 30-39 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 7931322-10 1994 Addition of the PKC inhibitor GF109203X blocked the down-regulation of MARCKS protein in PMA-treated cultures but not in retinoic acid-treated cells. Tetradecanoylphorbol Acetate 89-92 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 8166683-2 1994 It was found that the extent of TPA-induced phosphorylation of MARCKS was not significantly different between young and old IMR-90 fibroblasts. Tetradecanoylphorbol Acetate 32-35 myristoylated alanine rich protein kinase C substrate Homo sapiens 63-69 7963258-2 1994 Long-chain MACs (1-10 microM) strongly inhibited acetylcholine (ACh)-induced current (ACh-current); the block persisted for hours after washing the drugs out. Acetylcholine 49-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 11-15 7963258-2 1994 Long-chain MACs (1-10 microM) strongly inhibited acetylcholine (ACh)-induced current (ACh-current); the block persisted for hours after washing the drugs out. Acetylcholine 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 11-15 7963258-2 1994 Long-chain MACs (1-10 microM) strongly inhibited acetylcholine (ACh)-induced current (ACh-current); the block persisted for hours after washing the drugs out. Acetylcholine 86-89 myristoylated alanine rich protein kinase C substrate Homo sapiens 11-15 7963258-4 1994 Suppression of ACh-current by MACs was dose- and voltage-dependent; it was absent at low ACh doses or at potentials > or = 60 mV and increased with higher ACh doses or hyperpolarization. Acetylcholine 15-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-34 7963258-4 1994 Suppression of ACh-current by MACs was dose- and voltage-dependent; it was absent at low ACh doses or at potentials > or = 60 mV and increased with higher ACh doses or hyperpolarization. Acetylcholine 89-92 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-34 7963258-4 1994 Suppression of ACh-current by MACs was dose- and voltage-dependent; it was absent at low ACh doses or at potentials > or = 60 mV and increased with higher ACh doses or hyperpolarization. Acetylcholine 89-92 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-34 7963258-5 1994 The second of two ACh-currents induced by paired application of ACh was inhibited by long-chain MACs more strongly than the first. Acetylcholine 18-21 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-100 7963258-5 1994 The second of two ACh-currents induced by paired application of ACh was inhibited by long-chain MACs more strongly than the first. Acetylcholine 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-100 7963258-8 1994 Time constants of the recovery of the second ACh-current in the presence and after washing out of long-chain MACs were similar, ranging from 45 to 140 s at -50 mV for different long-chain MACs, and decreased with de- or hyperpolarization. Acetylcholine 45-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 109-113 7963258-8 1994 Time constants of the recovery of the second ACh-current in the presence and after washing out of long-chain MACs were similar, ranging from 45 to 140 s at -50 mV for different long-chain MACs, and decreased with de- or hyperpolarization. Acetylcholine 45-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 188-192 7963258-9 1994 The use-dependent block produced by long-chain MACs could be prevented by another long-chain MAC with a small ammonium head (IEM-1195, 75-100 microM) or trimethaphan (30 microM), a competitive antagonist of ACh in ganglia. Trimethaphan 153-165 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-51 7963258-9 1994 The use-dependent block produced by long-chain MACs could be prevented by another long-chain MAC with a small ammonium head (IEM-1195, 75-100 microM) or trimethaphan (30 microM), a competitive antagonist of ACh in ganglia. Acetylcholine 207-210 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-51 7963258-13 1994 We suggest that inhibition of ACh-current by long-chain MACs is accounted for by (i) a long-lasting, apparently irreversible, binding of the drug near the channel of nAChR via its long aliphatic chain and (ii) a slow reversible block of the nAChR channel with the MAC"s ammonium head. Acetylcholine 30-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-60 7957871-0 1994 Phosphorylation of synapsin I and MARCKS in nerve terminals is mediated by Ca2+ entry via an Aga-GI sensitive Ca2+ channel which is coupled to glutamate exocytosis. Glutamic Acid 143-152 myristoylated alanine rich protein kinase C substrate Homo sapiens 34-40 7957871-3 1994 Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. Potassium Chloride 29-32 myristoylated alanine rich protein kinase C substrate Homo sapiens 75-81 7891841-4 1994 The effect of glutamate is mimicked by phorbol esters and is markedly reduced by inhibitors of protein kinase C (PKC) such as staurosporine and calphostin C. PP80 has been identified by Western blot analysis as the PKC substrate MARCKS (myristoylated alanine-rich C kinase substrate), while antibody to GAP-43 (growth associated protein-43), the nervous tissue-specific substrate of PKC, failed to recognize PP43. Glutamic Acid 14-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 229-235 7891841-4 1994 The effect of glutamate is mimicked by phorbol esters and is markedly reduced by inhibitors of protein kinase C (PKC) such as staurosporine and calphostin C. PP80 has been identified by Western blot analysis as the PKC substrate MARCKS (myristoylated alanine-rich C kinase substrate), while antibody to GAP-43 (growth associated protein-43), the nervous tissue-specific substrate of PKC, failed to recognize PP43. Glutamic Acid 14-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 237-282 7891841-4 1994 The effect of glutamate is mimicked by phorbol esters and is markedly reduced by inhibitors of protein kinase C (PKC) such as staurosporine and calphostin C. PP80 has been identified by Western blot analysis as the PKC substrate MARCKS (myristoylated alanine-rich C kinase substrate), while antibody to GAP-43 (growth associated protein-43), the nervous tissue-specific substrate of PKC, failed to recognize PP43. Staurosporine 126-139 myristoylated alanine rich protein kinase C substrate Homo sapiens 229-235 7891841-4 1994 The effect of glutamate is mimicked by phorbol esters and is markedly reduced by inhibitors of protein kinase C (PKC) such as staurosporine and calphostin C. PP80 has been identified by Western blot analysis as the PKC substrate MARCKS (myristoylated alanine-rich C kinase substrate), while antibody to GAP-43 (growth associated protein-43), the nervous tissue-specific substrate of PKC, failed to recognize PP43. Staurosporine 126-139 myristoylated alanine rich protein kinase C substrate Homo sapiens 237-282 7531203-9 1994 Ultraviolet radiation induced a small increase in MARCKS protein phosphorylation but this effect was inhibited by pretreatment for 24 hours with 500 nM TPA, which had no effect on ultraviolet-induced melanogenesis. Tetradecanoylphorbol Acetate 152-155 myristoylated alanine rich protein kinase C substrate Homo sapiens 50-56 7918991-1 1994 Several groups have observed that phosphorylation causes the MARCKS (Myristoylated Alanine-Rich C Kinase Substrate) protein to move off cell membranes and phospholipid vesicles. Phospholipids 155-167 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 7918991-1 1994 Several groups have observed that phosphorylation causes the MARCKS (Myristoylated Alanine-Rich C Kinase Substrate) protein to move off cell membranes and phospholipid vesicles. Phospholipids 155-167 myristoylated alanine rich protein kinase C substrate Homo sapiens 69-114 7918991-6 1994 The electrostatic affinity of the MARCKS peptide for membranes containing 10% acidic phospholipids (10(4) M-1 = chi/[P], where chi is the mole ratio of peptide bound to the outer monolayer of the vesicles and [P] is the concentration of peptide in the aqueous phase) is the same as the hydrophobic affinity of the myristate moiety for bilayer membranes. Phospholipids 85-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 34-40 7918991-7 1994 Phosphorylation decreases the affinity of the MARCKS peptide for membranes containing 15% acidic lipid about 1000-fold and produces a rapid (t1/2 < 30 s) dissociation of the peptide from phospholipid vesicles. Phospholipids 190-202 myristoylated alanine rich protein kinase C substrate Homo sapiens 46-52 8132675-9 1994 These studies suggest that intact, recombinant MARCKS and MRP are accurately modeled by their synthetic PSCBD peptides with respect to PKC phosphorylation kinetics and their phosphorylation-dependent calmodulin binding properties. Peptides 110-118 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 8476618-13 1993 ED50 and ED95 for pancuronium with balanced anesthesia and for desflurane or isoflurane in low and high MACs, as well as speed of recovery, were determined. Isoflurane 77-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 104-108 7509863-6 1994 Of these three agonists, only TPA stimulated phosphorylation of MARCKS (225% of control), a specific substrate of PKC. Tetradecanoylphorbol Acetate 30-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 7514011-7 1994 Finally, in these cells, the phosphorylation of the endogenous PKC substrate, myristoylated alanine-rich C-kinase substrate (MARCKS), was slightly increased during several days, suggesting an involvement of PKC in the bFGF and IGF-I-induced differentiation. Alanine 92-99 myristoylated alanine rich protein kinase C substrate Homo sapiens 125-131 8408223-5 1993 The GAP-43 depletion procedure was specific for this protein and an antisense oligonucleotide to the related PKC substrate MARCKS did not detectably affect GAP-43 immunoreactivity. Oligonucleotides 78-93 myristoylated alanine rich protein kinase C substrate Homo sapiens 123-129 8486722-0 1993 Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. Phospholipids 92-105 myristoylated alanine rich protein kinase C substrate Homo sapiens 15-68 8486722-0 1993 Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. Phospholipids 92-105 myristoylated alanine rich protein kinase C substrate Homo sapiens 70-76 8486722-3 1993 MARCKS was found to bind to pure phospholipid membranes as well as to the synaptic vesicle membranes. Phospholipids 33-45 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8486722-7 1993 Phosphatidylserine but not phosphatidylcholine inhibited phosphorylation of MARCKS by protein kinase C. MARCKS seems to bind to the biomembranes through two binding sites: the N-terminal myristoyl moiety and the basic phosphorylation domain of amphiphilic nature. Phosphatidylserines 0-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 76-82 8486722-7 1993 Phosphatidylserine but not phosphatidylcholine inhibited phosphorylation of MARCKS by protein kinase C. MARCKS seems to bind to the biomembranes through two binding sites: the N-terminal myristoyl moiety and the basic phosphorylation domain of amphiphilic nature. Phosphatidylserines 0-18 myristoylated alanine rich protein kinase C substrate Homo sapiens 104-110 8313612-5 1994 This protein, myristoylated alanine-rich C kinase substrate ("MARCKS"), is implicated in synaptic neurotransmission, calcium regulation, and cytoskeletal restructuring. Calcium 117-124 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-69 8238525-6 1993 Stimulation of Caco-2 cell monolayers with phorbol myristate acetate or with the combination of carbachol and monolein was also associated with phosphorylation of the MARCKS protein, an endogenous substrate of PKC. Tetradecanoylphorbol Acetate 43-68 myristoylated alanine rich protein kinase C substrate Homo sapiens 167-173 8238525-6 1993 Stimulation of Caco-2 cell monolayers with phorbol myristate acetate or with the combination of carbachol and monolein was also associated with phosphorylation of the MARCKS protein, an endogenous substrate of PKC. Carbachol 96-105 myristoylated alanine rich protein kinase C substrate Homo sapiens 167-173 8489014-1 1993 MARCKS is a widespread cellular phosphoprotein that migrates at 80-87 kDa on polyacrylamide gels. polyacrylamide 77-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8489014-5 1993 MARCKS was found to be soluble in 40% acetic acid and can be extracted quantitatively and rapidly from phosphorylation mixtures in vitro or from labeled intact cells. Acetic Acid 38-49 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8489014-7 1993 Two extraction methods were developed, one for extraction of MARCKS from [gamma-32P]ATP-labeled subcellular fractions or intact synaptosomes labeled with 32Pi and one for extraction from 32Pi-labeled cultured nucleated cells, the latter requiring an additional protein recovery and DNA removal step. Adenosine Triphosphate 84-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 8437859-1 1993 Phorbol ester-inducible phosphorylation of MARCKS, the "80-kDa" substrate of protein kinase C, was undetectable in several phenotypically dominant, non-transformed revertants independently derived from the ras-transformed cell line NIH3T3 DT-ras. Phorbol Esters 0-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 43-49 8437859-3 1993 MARCKS-encoding mRNA levels were correspondingly decreased relative to normal and ras-transformed cells in all four ras revertant cell lines studied: C-11 and F-2, derived by 5-azacytidine treatment and selection with ouabain; CHP 9CJ, derived by ethylmethane sulfonate mutagenesis and selection with cis-hydroxy-L-proline; and 12-V3, derived by transfection with the human Krev-1 gene. Azacitidine 175-188 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8437859-3 1993 MARCKS-encoding mRNA levels were correspondingly decreased relative to normal and ras-transformed cells in all four ras revertant cell lines studied: C-11 and F-2, derived by 5-azacytidine treatment and selection with ouabain; CHP 9CJ, derived by ethylmethane sulfonate mutagenesis and selection with cis-hydroxy-L-proline; and 12-V3, derived by transfection with the human Krev-1 gene. Ethyl Methanesulfonate 247-269 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8437859-3 1993 MARCKS-encoding mRNA levels were correspondingly decreased relative to normal and ras-transformed cells in all four ras revertant cell lines studied: C-11 and F-2, derived by 5-azacytidine treatment and selection with ouabain; CHP 9CJ, derived by ethylmethane sulfonate mutagenesis and selection with cis-hydroxy-L-proline; and 12-V3, derived by transfection with the human Krev-1 gene. cis-4-hydroxyproline 301-322 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 8380584-5 1993 Exogenously added protein kinase C (PKC) also phosphorylated MARCKS and induced its translocation in the cells permeabilized with saponin. Saponins 130-137 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-67 8380584-4 1993 On the other hand, TPA treatment induced the phosphorylation and translocation of myristoylated alanine-rich C kinase substrate (MARCKS) from the membrane to the cytosol. Tetradecanoylphorbol Acetate 19-22 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-127 1400474-8 1992 Differential activities of PKC were also observed in synaptosol and in intact synaptosomes where PMA stimulated phosphorylation of MARCKS, but not dephosphin. Tetradecanoylphorbol Acetate 97-100 myristoylated alanine rich protein kinase C substrate Homo sapiens 131-137 8380584-4 1993 On the other hand, TPA treatment induced the phosphorylation and translocation of myristoylated alanine-rich C kinase substrate (MARCKS) from the membrane to the cytosol. Tetradecanoylphorbol Acetate 19-22 myristoylated alanine rich protein kinase C substrate Homo sapiens 129-135 1332970-3 1992 First, we showed that the MARCKS protein incorporated [3H]myristate when its mRNA was translated in vitro in reticulocyte lysates. Tritium 55-57 myristoylated alanine rich protein kinase C substrate Homo sapiens 26-32 1417956-10 1992 The phosphorylation of either by Ca/PS-activated kinase was nine times more potently inhibited by palmitoylcarnitine, while phosphorylation of MARCKS by PS/PMA-activated kinase was 10 times more potently inhibited by sphingosine. Palmitoylcarnitine 98-116 myristoylated alanine rich protein kinase C substrate Homo sapiens 143-149 1417956-10 1992 The phosphorylation of either by Ca/PS-activated kinase was nine times more potently inhibited by palmitoylcarnitine, while phosphorylation of MARCKS by PS/PMA-activated kinase was 10 times more potently inhibited by sphingosine. Sphingosine 217-228 myristoylated alanine rich protein kinase C substrate Homo sapiens 143-149 1378435-4 1992 In contrast, the effect of phorbol 12,13-dibutyrate on 80K/MARCKS mRNA levels was transient, and recovery of these transcripts correlated with the loss of PKC activity. Phorbol 12,13-Dibutyrate 27-51 myristoylated alanine rich protein kinase C substrate Homo sapiens 59-65 1643643-4 1992 Dose-response studies revealed that the most effective TPA concentration for stimulation of DNA synthesis and growth of melanocytes (10 ng/ml TPA) also supported a relatively high level of PKC enzyme activity, increased membrane association of the PKC alpha and PKC epsilon isoforms, and led to a high level of phosphorylation of a major PKC substrate, the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Tetradecanoylphorbol Acetate 55-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 357-402 1643643-4 1992 Dose-response studies revealed that the most effective TPA concentration for stimulation of DNA synthesis and growth of melanocytes (10 ng/ml TPA) also supported a relatively high level of PKC enzyme activity, increased membrane association of the PKC alpha and PKC epsilon isoforms, and led to a high level of phosphorylation of a major PKC substrate, the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Tetradecanoylphorbol Acetate 55-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 404-410 1643643-4 1992 Dose-response studies revealed that the most effective TPA concentration for stimulation of DNA synthesis and growth of melanocytes (10 ng/ml TPA) also supported a relatively high level of PKC enzyme activity, increased membrane association of the PKC alpha and PKC epsilon isoforms, and led to a high level of phosphorylation of a major PKC substrate, the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Tetradecanoylphorbol Acetate 142-145 myristoylated alanine rich protein kinase C substrate Homo sapiens 357-402 1643643-4 1992 Dose-response studies revealed that the most effective TPA concentration for stimulation of DNA synthesis and growth of melanocytes (10 ng/ml TPA) also supported a relatively high level of PKC enzyme activity, increased membrane association of the PKC alpha and PKC epsilon isoforms, and led to a high level of phosphorylation of a major PKC substrate, the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Tetradecanoylphorbol Acetate 142-145 myristoylated alanine rich protein kinase C substrate Homo sapiens 404-410 1643643-5 1992 Melanocytes incubated for 48 h with TPA at a higher concentration (100 ng/ml TPA) exhibited suboptimal TPA-stimulated DNA synthesis (28% of maximal) and decreased phosphorylation of the MARCKS substrate protein (50% of maximal). Tetradecanoylphorbol Acetate 36-39 myristoylated alanine rich protein kinase C substrate Homo sapiens 186-192 1643643-5 1992 Melanocytes incubated for 48 h with TPA at a higher concentration (100 ng/ml TPA) exhibited suboptimal TPA-stimulated DNA synthesis (28% of maximal) and decreased phosphorylation of the MARCKS substrate protein (50% of maximal). Tetradecanoylphorbol Acetate 77-80 myristoylated alanine rich protein kinase C substrate Homo sapiens 186-192 1643643-5 1992 Melanocytes incubated for 48 h with TPA at a higher concentration (100 ng/ml TPA) exhibited suboptimal TPA-stimulated DNA synthesis (28% of maximal) and decreased phosphorylation of the MARCKS substrate protein (50% of maximal). Tetradecanoylphorbol Acetate 77-80 myristoylated alanine rich protein kinase C substrate Homo sapiens 186-192 1378435-8 1992 Furthermore, elevation of cAMP, either through receptor-mediated mechanisms (e.g. prostaglandin E1) or by direct stimulation of adenylate cyclase (e.g. forskolin), also caused a marked dose-dependent depletion of 80K/MARCKS mRNA levels, which were further reduced by co-administration with cAMP-phosphodiesterase inhibitors. Colforsin 152-161 myristoylated alanine rich protein kinase C substrate Homo sapiens 217-223 1540183-3 1992 123 amino acids of ACAMP-81 were determined and the sequence was completely identical with that of MARCKS protein which was thought to be a substrate for calcium/phospholipid dependent protein kinase (PKC). acamp 19-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 99-105 1320036-9 1992 However, while prolonged PMA pretreatment ablates histamine-induced MARCKS phosphorylation, the ability of thrombin to induce MARCKS phosphorylation is retained. Histamine 50-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 68-74 1320036-5 1992 One micromolar histamine, like alpha-thrombin, produces sustained phosphorylation of MARCKS (plateau 3-5 min). Histamine 15-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 85-91 1320036-6 1992 In contrast, 100 microM histamine results in rapid but transient MARCKS phosphorylation (peak 1-3 min). Histamine 24-33 myristoylated alanine rich protein kinase C substrate Homo sapiens 65-71 1320036-8 1992 MARCKS phosphorylation can also be induced by several exogenous protein kinase C (PKC) activators and both alpha-thrombin- and histamine-induced MARCKS phosphorylation are inhibited by the PKC antagonist staurosporine. Histamine 127-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 1320036-8 1992 MARCKS phosphorylation can also be induced by several exogenous protein kinase C (PKC) activators and both alpha-thrombin- and histamine-induced MARCKS phosphorylation are inhibited by the PKC antagonist staurosporine. Histamine 127-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 145-151 1320036-8 1992 MARCKS phosphorylation can also be induced by several exogenous protein kinase C (PKC) activators and both alpha-thrombin- and histamine-induced MARCKS phosphorylation are inhibited by the PKC antagonist staurosporine. Staurosporine 204-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 1320036-8 1992 MARCKS phosphorylation can also be induced by several exogenous protein kinase C (PKC) activators and both alpha-thrombin- and histamine-induced MARCKS phosphorylation are inhibited by the PKC antagonist staurosporine. Staurosporine 204-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 145-151 1667426-6 1991 Based on own studies and literature data, the following MACs for asbestos and other natural fibrous minerals were established: a) for dusts containing asbestos and other fibrous minerals except crocidolite and fibrous antigorite, total dust concentration equals 1 mg/m3 and concentration of fibres longer than 5 microns = 0.5 fibre/cm3 b) for dusts containing crocidolite and fibrous antigorite total dust concentration = 0.5 mg/m3 and concentration of fibres longer than 5 microns = 0.2 fibre/cm3. Asbestos 65-73 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-60 1846353-4 1991 Bombesin induces the same extent of phosphorylation of MARCKS protein, the major cellular substrate for protein kinase C, irrespective of the medium calcium concentration for at least 4 h. Moreover, diverse cellular responses elicited by bombesin, including c-fos expression, activation of microtubule-associated protein 2 kinase and S6 kinase, glucose uptake, and protein synthesis but not the release of arachidonic acid and its metabolites, are induced similarly at either 0.03 or 3.0 mM calcium. Glucose 345-352 myristoylated alanine rich protein kinase C substrate Homo sapiens 55-61 1846353-4 1991 Bombesin induces the same extent of phosphorylation of MARCKS protein, the major cellular substrate for protein kinase C, irrespective of the medium calcium concentration for at least 4 h. Moreover, diverse cellular responses elicited by bombesin, including c-fos expression, activation of microtubule-associated protein 2 kinase and S6 kinase, glucose uptake, and protein synthesis but not the release of arachidonic acid and its metabolites, are induced similarly at either 0.03 or 3.0 mM calcium. Arachidonic Acid 406-422 myristoylated alanine rich protein kinase C substrate Homo sapiens 55-61 1846353-4 1991 Bombesin induces the same extent of phosphorylation of MARCKS protein, the major cellular substrate for protein kinase C, irrespective of the medium calcium concentration for at least 4 h. Moreover, diverse cellular responses elicited by bombesin, including c-fos expression, activation of microtubule-associated protein 2 kinase and S6 kinase, glucose uptake, and protein synthesis but not the release of arachidonic acid and its metabolites, are induced similarly at either 0.03 or 3.0 mM calcium. Calcium 491-498 myristoylated alanine rich protein kinase C substrate Homo sapiens 55-61 1435251-3 1992 Referring to literature, the authors present problems of exposure to asbestos, its production and MACs in Poland. Asbestos 69-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 98-102 1650359-1 1991 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine 113-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 33-78 1650359-1 1991 The phosphorylation sites in the myristoylated alanine-rich C kinase substrate or MARCKS protein consist of four serines contained within a conserved, basic region of 25 amino acids, termed the phosphorylation site domain. Serine 113-120 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 1650359-10 1991 Thus, the phosphorylation site domain peptide of the MARCKS protein is a high affinity substrate for protein kinase C in vitro; the cognate peptide containing no serines is a potent but not completely specific inhibitor of both protein kinase C and its catalytic fragment. Serine 162-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 1907204-10 1991 Stimulation of [32P]-prelabeled fibroblasts with serum, BK, vasopressin, or 12-O-tetradecanoyl phorbol acetate, but not epidermal growth factor or calcium ionophores, resulted in the rapid phosphorylation of MARCKS. Phosphorus-32 16-19 myristoylated alanine rich protein kinase C substrate Homo sapiens 208-214 1907204-10 1991 Stimulation of [32P]-prelabeled fibroblasts with serum, BK, vasopressin, or 12-O-tetradecanoyl phorbol acetate, but not epidermal growth factor or calcium ionophores, resulted in the rapid phosphorylation of MARCKS. Tetradecanoylphorbol Acetate 76-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 208-214 2145203-1 1990 Out of the whole number of impurities (more than 30) detected in aerosol discharge of TES using Cheliabinsk mine coal only for 16 of them MACs for the air of residentials areas or tentative safe exposure levels were established. TES 86-89 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-142 1844247-3 1991 Analysis of 32P-labelled phosphoproteins indicates that R6-PKC cells display increased phosphorylation of a 80/87 kDa protein (designated MARCKS), and after treatment with TPA they display a dramatic prolongation in the phosphorylation and in the cytosolic accumulation of this protein. Phosphorus-32 12-15 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-144 1844247-3 1991 Analysis of 32P-labelled phosphoproteins indicates that R6-PKC cells display increased phosphorylation of a 80/87 kDa protein (designated MARCKS), and after treatment with TPA they display a dramatic prolongation in the phosphorylation and in the cytosolic accumulation of this protein. Tetradecanoylphorbol Acetate 172-175 myristoylated alanine rich protein kinase C substrate Homo sapiens 138-144 2212950-0 1990 Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. Alanine 81-88 myristoylated alanine rich protein kinase C substrate Homo sapiens 66-79 2212950-4 1990 Activation of PKC with phorbol esters results in the rapid disappearance of punctate staining of MARCKS, but not vinculin or talin, and is accompanied by cell spreading and loss of filopodia. Phorbol Esters 23-37 myristoylated alanine rich protein kinase C substrate Homo sapiens 97-103 2241894-4 1990 Ca2(+)- and phospholipid-dependency of the phosphorylation in vitro confirmed that both 80K-L and 80K-H proteins are true substrates for three subtypes of protein kinase C. The 80K-L protein was a preferential substrate for type III protein kinase C, and the 80K-H protein was phosphorylated more effectively by type I and type II protein kinase C. The possible roles of these two distinct 80K proteins in signal transduction are discussed. Phospholipids 12-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 88-93 2241894-4 1990 Ca2(+)- and phospholipid-dependency of the phosphorylation in vitro confirmed that both 80K-L and 80K-H proteins are true substrates for three subtypes of protein kinase C. The 80K-L protein was a preferential substrate for type III protein kinase C, and the 80K-H protein was phosphorylated more effectively by type I and type II protein kinase C. The possible roles of these two distinct 80K proteins in signal transduction are discussed. Phospholipids 12-24 myristoylated alanine rich protein kinase C substrate Homo sapiens 177-182 34396878-8 2021 CONCLUSIONS: We conclude that the Chinese version of EDACS is valid and reliable to be easily used by health professionals and teachers to classify functional eating and drinking abilities in children with cerebral palsy.IMPLICATIONS FOR REHABILITATIONThe Chinese version of EDACS is valid and reliable to be easily used.EDACS can be used by health professionals and teachers to classify functional eating and drinking abilities in children with cerebral palsy.The EDACS is analogous to other functional classification systems (i.e., GMFCS, MACS and CFCS) and specifically represents eating and drinking ability. edacs 53-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 541-545 34753776-12 2021 CONCLUSION: HEAR and HE-MACS show potential as rule out tools for acute myocardial infarction without the need for troponin testing. Helium 21-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 24-28 34556581-10 2021 This approach identifies myristoylated alanine-rich C-kinase substrate (MARCKS) as a putative d-cysteine-binding protein. D-cysteine 94-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 25-70 34556581-10 2021 This approach identifies myristoylated alanine-rich C-kinase substrate (MARCKS) as a putative d-cysteine-binding protein. D-cysteine 94-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 2210426-3 1990 MACs for anthraquinones, alpha-aminoanthraquinones and K-type dispersal dye-stuff were established at 5 mg/m3. Anthraquinones 9-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-4 2210426-6 1990 The group MACs for the pigment and NF disperser containing dispersal anthraquinone dye-stuffs at 5 mg/m3 was established and subsequently formally adopted. Anthraquinones 69-82 myristoylated alanine rich protein kinase C substrate Homo sapiens 10-14 34509657-3 2021 MARCKS can sequester phosphatidylinositol-4, 5-diphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C (PKC), ultimately modulating the immune function. Phosphatidylinositol 4,5-Diphosphate 21-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 34509657-3 2021 MARCKS can sequester phosphatidylinositol-4, 5-diphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C (PKC), ultimately modulating the immune function. Phosphatidylinositol 4,5-Diphosphate 60-64 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 34279157-14 2021 CONCLUSION: The present study suggests that MARCKS on TAMs is associated with poor prognosis and immune cell infiltration in HCC. tams 54-58 myristoylated alanine rich protein kinase C substrate Homo sapiens 44-50 34083252-7 2021 Our data also indicate that MACs release glycine at conventional chemical synapses, and viral retrograde transsynaptic tracing from the dorsal lateral geniculate nucleus (dLGN) showed selective connections between MACs and a subpopulation of RGC types. Glycine 41-48 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-32 35484375-4 2022 D-cysteine binds to MARCKS and a host of proteins implicated in cell division and neurodevelopmental disorders. D-cysteine 0-10 myristoylated alanine rich protein kinase C substrate Homo sapiens 20-26 35589403-6 2022 Furthermore, another study investigated noticed that MACS after tracer injection facilitated determination of high 18F-FDG uptake in myeloid cells in a range of tumor models. Fluorodeoxyglucose F18 115-122 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-57 35484375-5 2022 D-cysteine decreases phosphorylation of MARCKS in neural progenitor cells (NPCs) affecting its translocation. D-cysteine 0-10 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 35158093-9 2022 MARCKS was phosphorylated on stimulation of SKOV-3 cells with EGF that was inhibited by Lapatinib and CP724714 which was dependent on the kinase activity of ErbB2. Lapatinib 88-97 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 35158093-9 2022 MARCKS was phosphorylated on stimulation of SKOV-3 cells with EGF that was inhibited by Lapatinib and CP724714 which was dependent on the kinase activity of ErbB2. 2-methoxy-N-(3-(4-((3-methyl-4-((6-methyl-3-pyridinyl)oxy)phenyl)amino)-6-quinazolinyl)-2-propenyl)acetamide 102-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 35157693-0 2022 gmxapi: A GROMACS-native Python interface for molecular dynamics with ensemble and plugin support. gmxapi 0-6 myristoylated alanine rich protein kinase C substrate Homo sapiens 10-17 35157693-1 2022 Gmxapi provides an integrated, native Python API for both standard and advanced molecular dynamics simulations in GROMACS. gmxapi 0-6 myristoylated alanine rich protein kinase C substrate Homo sapiens 114-121 32356316-3 2020 Mechanistically, MA suppressed U46619- or ADP-induced phosphorylation of myristoylated alanine-rich C kinase substrate, and the expression of P-selectin, and activated PAC-1 in platelets. 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid 31-37 myristoylated alanine rich protein kinase C substrate Homo sapiens 73-118 33668794-2 2021 The aim of our study is to assess the expression of previously described genes that may influence the resistance to bortezomib treatment at the mRNA level (ABCB1, CXCR4, MAF, MARCKS, POMP, PSMB5, RPL5, TXN, and XBP1) and prognosis of MM patients. Bortezomib 116-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 175-181 33958003-2 2021 Functioning as a target of protein kinase C, MARCKS shuttles between the phosphorylated cytosolic form and the unphosphorylated plasma membrane-bound states whilst regulating several molecular partners including, but not limited to calmodulin, actin, phosphatidylinositol-4,5-bisphosphate, and phosphoinositide-3-kinase. Phosphatidylinositol 4,5-Diphosphate 251-288 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-51 33735912-9 2021 MARCKS sequesters PIP2, thereby affecting central signaling pathways and clustering of the B cell receptor. Phosphatidylinositol 4,5-Diphosphate 18-22 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 33735912-13 2021 In line with our in vitro findings, low MARCKS expression is associated with significantly higher treatment-induced leukocytosis and more pronounced decrease of nodal disease in CLL patients treated with acalabrutinib. acalabrutinib 204-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 40-46 33578797-5 2021 Notably, myristoylated alanine-rich C-kinase substrate (MARCKS) and Wntless homolog protein (WLS) were upregulated in oxaliplatin-resistant cells compared to sensitive cells, as confirmed by qRT-PCR and Western blot analysis. Oxaliplatin 118-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-54 33578797-5 2021 Notably, myristoylated alanine-rich C-kinase substrate (MARCKS) and Wntless homolog protein (WLS) were upregulated in oxaliplatin-resistant cells compared to sensitive cells, as confirmed by qRT-PCR and Western blot analysis. Oxaliplatin 118-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 33578797-6 2021 We further demonstrated the activation of AKT and beta-catenin signaling (downstream targets of MARCKS and WLS, respectively) in oxaliplatin-resistant PANC-1 cells. Oxaliplatin 129-140 myristoylated alanine rich protein kinase C substrate Homo sapiens 96-102 33578797-7 2021 Additionally, we show that the siRNA-mediated suppression of both MARCKS and WLS enhanced oxaliplatin sensitivity in oxaliplatin-resistant PANC-1 cells. Oxaliplatin 90-101 myristoylated alanine rich protein kinase C substrate Homo sapiens 66-72 33578797-7 2021 Additionally, we show that the siRNA-mediated suppression of both MARCKS and WLS enhanced oxaliplatin sensitivity in oxaliplatin-resistant PANC-1 cells. Oxaliplatin 117-128 myristoylated alanine rich protein kinase C substrate Homo sapiens 66-72 33578797-8 2021 Taken together, our results provide insights into multiple mechanisms of oxaliplatin resistance in pancreatic cancer cells and reveal that MARCKS and WLS might be involved in the oxaliplatin resistance. Oxaliplatin 179-190 myristoylated alanine rich protein kinase C substrate Homo sapiens 139-145 32652421-2 2021 The laccase was immobilized on magnetic chitosan nanoparticles modified with amino-functionalized ionic liquid containing ABTS (MACS-NIL) based on Cu ion chelation (MACS-NIL-Cu-lac). ABTS diammonium salt 122-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 128-132 32652421-2 2021 The laccase was immobilized on magnetic chitosan nanoparticles modified with amino-functionalized ionic liquid containing ABTS (MACS-NIL) based on Cu ion chelation (MACS-NIL-Cu-lac). ABTS diammonium salt 122-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 165-169 32652421-2 2021 The laccase was immobilized on magnetic chitosan nanoparticles modified with amino-functionalized ionic liquid containing ABTS (MACS-NIL) based on Cu ion chelation (MACS-NIL-Cu-lac). Copper 147-149 myristoylated alanine rich protein kinase C substrate Homo sapiens 128-132 32652421-2 2021 The laccase was immobilized on magnetic chitosan nanoparticles modified with amino-functionalized ionic liquid containing ABTS (MACS-NIL) based on Cu ion chelation (MACS-NIL-Cu-lac). Copper 147-149 myristoylated alanine rich protein kinase C substrate Homo sapiens 165-169 32652421-5 2021 The removal performance assay found that MACS-NIL-Cu-lac had a good removal efficiency with 100.0 % for 2,4-dichlorophenol in water at 25 C, even when the concentration reached 50 mg/L. 2,4-dichlorophenol 104-122 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-45 32652421-5 2021 The removal performance assay found that MACS-NIL-Cu-lac had a good removal efficiency with 100.0 % for 2,4-dichlorophenol in water at 25 C, even when the concentration reached 50 mg/L. Water 126-131 myristoylated alanine rich protein kinase C substrate Homo sapiens 41-45 32652421-6 2021 Reusability study showed that after six catalytic runs, the removal efficiency of 2,4-dichlorophenol by MACS-NIL-Cu-lac could still reach 93.2 %. 2,4-dichlorophenol 82-100 myristoylated alanine rich protein kinase C substrate Homo sapiens 104-108 32652421-7 2021 Additionally, MACS-NIL-Cu-lac exhibited higher catalytic efficiencies with 100.0 %, 70.5 % and 93.3 % for bisphenol A, indole, and anthracene, respectively. bisphenol A 106-117 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-18 32652421-7 2021 Additionally, MACS-NIL-Cu-lac exhibited higher catalytic efficiencies with 100.0 %, 70.5 % and 93.3 % for bisphenol A, indole, and anthracene, respectively. indole 119-125 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-18 32652421-7 2021 Additionally, MACS-NIL-Cu-lac exhibited higher catalytic efficiencies with 100.0 %, 70.5 % and 93.3 % for bisphenol A, indole, and anthracene, respectively. anthracene 131-141 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-18 33125657-4 2021 In this chapter, we shall discuss the methods to parameterize a fluorescent probe (fluorescein) attached to a cysteine, as a modified residue, for performing simulations with GROMACS. Fluorescein 83-94 myristoylated alanine rich protein kinase C substrate Homo sapiens 175-182 33125657-4 2021 In this chapter, we shall discuss the methods to parameterize a fluorescent probe (fluorescein) attached to a cysteine, as a modified residue, for performing simulations with GROMACS. Cysteine 110-118 myristoylated alanine rich protein kinase C substrate Homo sapiens 175-182 33046669-3 2020 Methods: We reviewed the clinical records of 6 patients with the Interagency Registry for Mechanically Assisted Circulatory Support (INTERMACS) profile 1, awaiting heart transplantation, who were provided with temporary e-VAD from 2018 to 2019. e-vad 220-225 myristoylated alanine rich protein kinase C substrate Homo sapiens 133-142 33046669-11 2020 Conclusion: e-VAD may reverse end-organ dysfunction and improve outcomes in INTERMACS I heart transplant patients. e-vad 12-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 76-85 32356316-3 2020 Mechanistically, MA suppressed U46619- or ADP-induced phosphorylation of myristoylated alanine-rich C kinase substrate, and the expression of P-selectin, and activated PAC-1 in platelets. Adenosine Diphosphate 42-45 myristoylated alanine rich protein kinase C substrate Homo sapiens 73-118 33077834-3 2020 Because almost all GBM tumors have dysregulated phosphoinositide signaling as part of that process, we hypothesized that peptide mimetics derived from the phospholipid binding domain of Myristoylated alanine-rich C-kinase substrate (MARCKS) could serve as a novel GBM therapeutic. Phosphatidylinositols 48-64 myristoylated alanine rich protein kinase C substrate Homo sapiens 186-231 32056006-4 2020 The protein Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is a pivotal regulator of PI(4,5)P2 and inactivated in many CRC cancers via genetic deletion or hyperphosphorylation. pi(4,5)p2 93-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 12-57 32056006-13 2020 In CRC cells, bosutinib treatment resulted in a MARCKS translocation from the cytosol to the plasma membrane, while simultaneously, ABCB1 was relocated to intracellular compartments. bosutinib 14-23 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 32707323-0 2020 MARCKS mediates vascular contractility through regulating interactions between voltage-gated Ca2+ channels and PIP2. Phosphatidylinositol 4,5-Diphosphate 111-115 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 32707323-4 2020 Knockdown of MARCKS using morpholino oligonucleotides reduced contractions induced by MANS and stimulation of alpha1-adrenoceptors and thromboxane receptors with methoxamine (MO) and U46619 respectively. Morpholinos 26-53 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 32707323-4 2020 Knockdown of MARCKS using morpholino oligonucleotides reduced contractions induced by MANS and stimulation of alpha1-adrenoceptors and thromboxane receptors with methoxamine (MO) and U46619 respectively. Methoxamine 162-173 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 32707323-4 2020 Knockdown of MARCKS using morpholino oligonucleotides reduced contractions induced by MANS and stimulation of alpha1-adrenoceptors and thromboxane receptors with methoxamine (MO) and U46619 respectively. 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid 183-189 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 32707323-6 2020 Dot-blots revealed greater PIP2 binding to MARCKS than CaV1.2 in unstimulated tissue, with this binding profile reversed following stimulation by MANS and MO. Phosphatidylinositol 4,5-Diphosphate 27-31 myristoylated alanine rich protein kinase C substrate Homo sapiens 43-49 32707323-8 2020 This present study indicates for the first time that MARCKS is important regulating vascular contractility and suggests that disinhibition of MARCKS by MANS or vasoconstrictors may induce contraction through releasing PIP2 into the local environment where it increases voltage-gated Ca2+ channel activity. Phosphatidylinositol 4,5-Diphosphate 218-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 53-59 32707323-8 2020 This present study indicates for the first time that MARCKS is important regulating vascular contractility and suggests that disinhibition of MARCKS by MANS or vasoconstrictors may induce contraction through releasing PIP2 into the local environment where it increases voltage-gated Ca2+ channel activity. Phosphatidylinositol 4,5-Diphosphate 218-222 myristoylated alanine rich protein kinase C substrate Homo sapiens 142-148 32220540-8 2020 In accordance, combined treatment with MARCKS antagonists, bortezomib and the autophagy inhibitor, chloroquine, significantly diminished tumor growth in drug-resistant MM cell lines as well as primary MM cells. Chloroquine 99-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 39-45 32056006-14 2020 Inhibition of MARCKS phosphorylation via bosutinib rendered cells more sensitive to the chemotherapeutics doxorubicin and 5-FU. bosutinib 41-50 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 32056006-14 2020 Inhibition of MARCKS phosphorylation via bosutinib rendered cells more sensitive to the chemotherapeutics doxorubicin and 5-FU. Doxorubicin 106-117 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 32056006-4 2020 The protein Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) is a pivotal regulator of PI(4,5)P2 and inactivated in many CRC cancers via genetic deletion or hyperphosphorylation. pi(4,5)p2 93-102 myristoylated alanine rich protein kinase C substrate Homo sapiens 59-65 32056006-14 2020 Inhibition of MARCKS phosphorylation via bosutinib rendered cells more sensitive to the chemotherapeutics doxorubicin and 5-FU. Fluorouracil 122-126 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 31936855-6 2020 This PKC- and PIP2-mediated gating mechanism is regulated by the PIP2-binding protein myristoylated alanine-rich C kinase (MARCKS) and is coupled to store depletion by TRPC1-STIM1 interactions which induce Gq/PLCbeta1 activity. Alanine 100-107 myristoylated alanine rich protein kinase C substrate Homo sapiens 123-129 32021440-2 2020 Allylated monocarbonyl analogs of curcumin (MACs) have been reported to selectively inhibit a broad range of human cancers including gastric cancer. B19 monocarbonyl curcumin 10-22 myristoylated alanine rich protein kinase C substrate Homo sapiens 44-48 32021440-2 2020 Allylated monocarbonyl analogs of curcumin (MACs) have been reported to selectively inhibit a broad range of human cancers including gastric cancer. Curcumin 34-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 44-48 30655546-3 2019 Here, we show that high maternal glucose induced MARCKS acetylation at lysine 165 by the acetyltransferase Tip60, which is a prerequisite for its phosphorylation, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS. Glucose 33-40 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 31373006-0 2019 Morphine contributed to the deterioration of cancer via miR-543/MARCKS/FcgammaR-mediated phagocytosis pathway. Morphine 0-8 myristoylated alanine rich protein kinase C substrate Homo sapiens 64-70 31373006-4 2019 KEY FINDINGS: Bioinformatics analysis identified that downregulation of MARCKS and upregulation of miR-543 in samples treated with morphine. Morphine 131-139 myristoylated alanine rich protein kinase C substrate Homo sapiens 72-78 31373006-12 2019 CONCLUSIONS: Morphine at 10-6 mol/l could benefit miR-543 expression to inhibit MARCKS expression, consequently, blocking FcgammaR-mediated phagocytosis pathway, which contributed to the cancer progression in vitro and in vivo. Morphine 13-21 myristoylated alanine rich protein kinase C substrate Homo sapiens 81-87 30942445-2 2019 Myristoylated alanine-rich C-kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)-bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while also serving as a nuclear localization sequence. Phospholipids 204-216 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 30942445-2 2019 Myristoylated alanine-rich C-kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)-bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while also serving as a nuclear localization sequence. Phosphatidylinositol 4,5-Diphosphate 217-256 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 30942445-2 2019 Myristoylated alanine-rich C-kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)-bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while also serving as a nuclear localization sequence. Phosphatidylinositol 4,5-Diphosphate 258-262 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 30942445-2 2019 Myristoylated alanine-rich C-kinase substrate (MARCKS) is a 32 kDa intrinsically unstructured protein containing a polybasic (+13) effector domain (ED), which regulates its electrostatic sequestration of phospholipid phosphatidylinositol (4,5)-bisphosphate (PIP2), and its binding to phosphatidylserine, calcium/calmodulin, filamentous actin, while also serving as a nuclear localization sequence. Phosphatidylserines 284-302 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 31058089-3 2019 GAP43, MARCKS, and BASP1 bind to cell membrane phospholipids, a process reversibly regulated by protein kinase C-phosphorylation or by binding to the calcium sensor calmodulin (CaM). Phospholipids 47-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 7-13 30703330-4 2019 Herein, we report that an exosome-targeting prodrug system, designated MARCKS-ED-photodoxaz, could spatiotemporally control the activation of an exquisitely cytotoxic agent, doxazolidine (doxaz), with UV light. doxazolidine 174-186 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 30703330-4 2019 Herein, we report that an exosome-targeting prodrug system, designated MARCKS-ED-photodoxaz, could spatiotemporally control the activation of an exquisitely cytotoxic agent, doxazolidine (doxaz), with UV light. doxazolidine 86-91 myristoylated alanine rich protein kinase C substrate Homo sapiens 71-77 30703330-6 2019 MARCKS-ED-photodoxaz releases doxaz under near-UV irradiation to inhibit cell growth with low nanomolar IC50 values. doxazolidine 15-20 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 30929966-18 2019 In the presence of cycloheximide, MARCKS knockdown in VSMCs decreased KIS protein stability but had no effect in ECs. Cycloheximide 19-32 myristoylated alanine rich protein kinase C substrate Homo sapiens 34-40 30929966-19 2019 The effect of MARCKS knockdown on KIS stability was abrogated by the 26s proteasome inhibitor MG-132. benzyloxycarbonylleucyl-leucyl-leucine aldehyde 94-100 myristoylated alanine rich protein kinase C substrate Homo sapiens 14-20 30929966-23 2019 Furthermore, MARCKS knockdown in vivo resulted in decreased 5-ethynyl-2"-deoxyuridine integration and significantly reduced intimal thickening. 5-ethynyl-2'-deoxyuridine 60-85 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 30942445-4 2019 In the present study, using a tetracycline-inducible system in PTEN-null U87 cells, we demonstrate that MARCKS overexpression suppresses growth and enhances radiation sensitivity in vivo. Tetracycline 30-42 myristoylated alanine rich protein kinase C substrate Homo sapiens 104-110 30655546-3 2019 Here, we show that high maternal glucose induced MARCKS acetylation at lysine 165 by the acetyltransferase Tip60, which is a prerequisite for its phosphorylation, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS. Glucose 33-40 myristoylated alanine rich protein kinase C substrate Homo sapiens 202-208 30655546-3 2019 Here, we show that high maternal glucose induced MARCKS acetylation at lysine 165 by the acetyltransferase Tip60, which is a prerequisite for its phosphorylation, whereas Sirtuin 2 (SIRT2) deacetylated MARCKS. Lysine 71-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 49-55 29715315-4 2018 A hypothesis explaining this link emerged, postulating that Ca2+-activated PKC displaces the MARCKS protein from plasma membrane PIP2, thereby releasing sequestered PIP2 to serve as the target and substrate lipid of PI3K in PIP3 production. Phosphatidylinositol 4,5-Diphosphate 129-133 myristoylated alanine rich protein kinase C substrate Homo sapiens 93-99 30225819-4 2018 A significant positive correlation (r = 0.772, P = 0.000) was apparent between the level of SDF in the NEAT ejaculate and the efficacy of SDF reduction observed in the MACS- fraction. [(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid 92-95 myristoylated alanine rich protein kinase C substrate Homo sapiens 168-172 30225819-4 2018 A significant positive correlation (r = 0.772, P = 0.000) was apparent between the level of SDF in the NEAT ejaculate and the efficacy of SDF reduction observed in the MACS- fraction. [(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid 138-141 myristoylated alanine rich protein kinase C substrate Homo sapiens 168-172 30225819-5 2018 CONCLUSION: MACS is capable of reducing the proportion of SDF, especially spermatozoa with a highly degraded DNA molecule. [(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid 58-61 myristoylated alanine rich protein kinase C substrate Homo sapiens 12-16 30225819-7 2018 The MACS protocol was two- to threefold more efficient when the SDF in NEAT ejaculate was equal to or greater than 30%. [(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 4-8 30225819-8 2018 In 4 of 20 individuals, the level of SDF after MACS resulted in semen for ICSI with a higher or non-significant reduction when compared to SDF observed in the NEAT ejaculate. [(R)-(2,4-dichlorophenyl)(sulfanyl)methyl]phosphonic acid 37-40 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-51 29715315-4 2018 A hypothesis explaining this link emerged, postulating that Ca2+-activated PKC displaces the MARCKS protein from plasma membrane PIP2, thereby releasing sequestered PIP2 to serve as the target and substrate lipid of PI3K in PIP3 production. Phosphatidylinositol 4,5-Diphosphate 165-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 93-99 29715315-4 2018 A hypothesis explaining this link emerged, postulating that Ca2+-activated PKC displaces the MARCKS protein from plasma membrane PIP2, thereby releasing sequestered PIP2 to serve as the target and substrate lipid of PI3K in PIP3 production. PIP3 224-228 myristoylated alanine rich protein kinase C substrate Homo sapiens 93-99 28623606-4 2017 Enhanced MARCKS phosphorylation by Nogo66 or myelin debris treatment inhibited OPC maturation, while its dephosphorylation by protein phosphatase 2 A activator D-erythro-sphingosine promoted OPC development in the presence of myelin debris. Deuterium 160-161 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-15 28623606-4 2017 Enhanced MARCKS phosphorylation by Nogo66 or myelin debris treatment inhibited OPC maturation, while its dephosphorylation by protein phosphatase 2 A activator D-erythro-sphingosine promoted OPC development in the presence of myelin debris. erythro-(2R,3S)-sphingosine 162-181 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-15 27349763-0 2016 MARCKS is involved in methylmercury-induced decrease in cell viability and nitric oxide production in EA.hy926 cells. Nitric Oxide 75-87 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 28166200-7 2017 Following knockdown of MARCKS in RCC cells, the IC50 of the multikinase inhibitor regorafenib was reduced. regorafenib 82-93 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-29 28166200-8 2017 Surprisingly, attenuation of MARCKS using the MPS (MARCKS phosphorylation site domain) peptide synergistically interacted with regorafenib treatment and decreased survival of kidney cancer cells through inactivation of AKT and mTOR. regorafenib 127-138 myristoylated alanine rich protein kinase C substrate Homo sapiens 29-35 28166200-8 2017 Surprisingly, attenuation of MARCKS using the MPS (MARCKS phosphorylation site domain) peptide synergistically interacted with regorafenib treatment and decreased survival of kidney cancer cells through inactivation of AKT and mTOR. regorafenib 127-138 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 28422723-7 2017 Multivariate analysis revealed that MACs without both SAC morphology and CIMP-positive status exhibited 3.955 times greater risk of cancer relapse than MACs having both characteristics or either one (P=0.035). Cyclic IMP 73-77 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-40 27933776-4 2016 A previous study implicated Ca2+-activated protein kinase C (PKC) and the phosphatidylinositol 4,5-bisphosphate (PIP2) binding protein MARCKS as two important players in this signaling, because PKC phosphorylation of MARCKS releases free PIP2 that serves as the membrane binding target and substrate for PI3K. Phosphatidylinositol 4,5-Diphosphate 74-111 myristoylated alanine rich protein kinase C substrate Homo sapiens 135-141 27933776-4 2016 A previous study implicated Ca2+-activated protein kinase C (PKC) and the phosphatidylinositol 4,5-bisphosphate (PIP2) binding protein MARCKS as two important players in this signaling, because PKC phosphorylation of MARCKS releases free PIP2 that serves as the membrane binding target and substrate for PI3K. Phosphatidylinositol 4,5-Diphosphate 74-111 myristoylated alanine rich protein kinase C substrate Homo sapiens 217-223 27933776-4 2016 A previous study implicated Ca2+-activated protein kinase C (PKC) and the phosphatidylinositol 4,5-bisphosphate (PIP2) binding protein MARCKS as two important players in this signaling, because PKC phosphorylation of MARCKS releases free PIP2 that serves as the membrane binding target and substrate for PI3K. Phosphatidylinositol 4,5-Diphosphate 113-117 myristoylated alanine rich protein kinase C substrate Homo sapiens 135-141 27933776-4 2016 A previous study implicated Ca2+-activated protein kinase C (PKC) and the phosphatidylinositol 4,5-bisphosphate (PIP2) binding protein MARCKS as two important players in this signaling, because PKC phosphorylation of MARCKS releases free PIP2 that serves as the membrane binding target and substrate for PI3K. Phosphatidylinositol 4,5-Diphosphate 113-117 myristoylated alanine rich protein kinase C substrate Homo sapiens 217-223 27933776-4 2016 A previous study implicated Ca2+-activated protein kinase C (PKC) and the phosphatidylinositol 4,5-bisphosphate (PIP2) binding protein MARCKS as two important players in this signaling, because PKC phosphorylation of MARCKS releases free PIP2 that serves as the membrane binding target and substrate for PI3K. Phosphatidylinositol 4,5-Diphosphate 238-242 myristoylated alanine rich protein kinase C substrate Homo sapiens 135-141 27542283-4 2016 MARCKS upregulation was confirmed on protein level and also observed in other BTZ-resistant tumor cell lines as well as in leukemia cells with acquired resistance to other proteasome inhibitors. Bortezomib 78-81 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 27542283-5 2016 Moreover, when MARCKS protein expression was demonstrated in specimens derived from therapy-refractory pediatric leukemia patients (n = 44), higher MARCKS protein expression trended (p = 0.073) towards a dismal response to BTZ-containing chemotherapy. Bortezomib 223-226 myristoylated alanine rich protein kinase C substrate Homo sapiens 15-21 27542283-5 2016 Moreover, when MARCKS protein expression was demonstrated in specimens derived from therapy-refractory pediatric leukemia patients (n = 44), higher MARCKS protein expression trended (p = 0.073) towards a dismal response to BTZ-containing chemotherapy. Bortezomib 223-226 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-154 27542283-6 2016 Mechanistically, we show a BTZ concentration-dependent association of MARCKS protein levels with the emergence of ubiquitin-containing vesicles in BTZ-resistant CEM cells. Bortezomib 27-30 myristoylated alanine rich protein kinase C substrate Homo sapiens 70-76 27542283-6 2016 Mechanistically, we show a BTZ concentration-dependent association of MARCKS protein levels with the emergence of ubiquitin-containing vesicles in BTZ-resistant CEM cells. Bortezomib 147-150 myristoylated alanine rich protein kinase C substrate Homo sapiens 70-76 27542283-8 2016 Consistent with these observations, MARCKS protein associated with ubiquitin-containing vesicles was also more prominent in clinical leukemic specimen with ex vivo BTZ resistance compared to BTZ-sensitive leukemia cells. Bortezomib 164-167 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 27542283-8 2016 Consistent with these observations, MARCKS protein associated with ubiquitin-containing vesicles was also more prominent in clinical leukemic specimen with ex vivo BTZ resistance compared to BTZ-sensitive leukemia cells. Bortezomib 191-194 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 27542283-9 2016 Collectively, we propose a role for MARCKS in a novel mechanism of BTZ resistance via exocytosis of ubiquitinated proteins in BTZ-resistant cells leading to quenching of proteolytic stress. Bortezomib 67-70 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 27542283-9 2016 Collectively, we propose a role for MARCKS in a novel mechanism of BTZ resistance via exocytosis of ubiquitinated proteins in BTZ-resistant cells leading to quenching of proteolytic stress. Bortezomib 126-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 36-42 27119641-4 2016 Our findings demonstrate that together Ca(2+)-PKC and the PIP2-binding peptide of MARCKS modulate the level of free PIP2, which serves as both a docking target and substrate lipid for PI3K. Phosphatidylinositol 4,5-Diphosphate 58-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 82-88 27004748-3 2016 METHOD: The growth, morphology, cell cycle regulation, apoptosis induction and angiogenesis of oral cancer cell lines (SCC-4, SCC-9, SCC-25) via MACS-purified Treg cells were performed by MTT, propidium iodide (PI) staining, annexin-V-binding assay and ELISA respectively. monooxyethylene trimethylolpropane tristearate 188-191 myristoylated alanine rich protein kinase C substrate Homo sapiens 145-149 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Lysine 56-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-22 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Lysine 56-59 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-113 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Phenylalanine 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 16-22 27166806-4 2016 Research of the MARCKS-ED has further revealed that its Lys and Phe residues play an essential role in how MARCKS-ED detects and binds to curved bilayers. Phenylalanine 64-67 myristoylated alanine rich protein kinase C substrate Homo sapiens 107-113 27092941-6 2016 Finally, 4-ipomeanol efficiently induced apoptosis in primary T cells that co-express mutant CYP4B1 and the divergently located MACS selection and CAR genes. 4-ipomeanol 9-20 myristoylated alanine rich protein kinase C substrate Homo sapiens 128-132 27119641-6 2016 In the on state, Ca(2+)-PKC phosphorylation of the MARCKS peptide reverses the PIP2 sequestration, thereby releasing multiple PIP2 molecules that recruit multiple active PI3K molecules to the membrane surface. Phosphatidylinositol 4,5-Diphosphate 79-83 myristoylated alanine rich protein kinase C substrate Homo sapiens 51-57 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 101-141 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-44 26650714-0 2016 Differential interaction of beta2e with phosphoinositides: A comparative study between beta2e and MARCKS. Phosphatidylinositols 40-57 myristoylated alanine rich protein kinase C substrate Homo sapiens 98-104 26650714-7 2016 First, the charge neutralization of the inner leaf of the plasma membrane induced the translocation of both beta2e and MARCKS to the cytosol, while the transient depletion of poly-phosphoinositides (poly-PIs) by translocatable pseudojanin (PJ) systems induced the cytosolic translocation of beta2e but not MARCKS. Phosphatidylinositol Phosphates 199-207 myristoylated alanine rich protein kinase C substrate Homo sapiens 306-312 26650714-9 2016 We also found that after the cytosolic translocation of MARCKS by receptor activation, depletion of poly-PIs slowed the recovery of MARCKS to the plasma membrane. Phosphatidylinositol Phosphates 100-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 26650714-9 2016 We also found that after the cytosolic translocation of MARCKS by receptor activation, depletion of poly-PIs slowed the recovery of MARCKS to the plasma membrane. Phosphatidylinositol Phosphates 100-108 myristoylated alanine rich protein kinase C substrate Homo sapiens 132-138 26443186-5 2016 Vinorelbine and epirubicin stimulate neurite outgrowth of cerebellar neurons via the neural cell adhesion molecule, via myristoylated alanine-rich C kinase substrate, and via fibroblast growth factor receptor, signaling through Erk pathways. Vinorelbine 0-11 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-165 26443186-5 2016 Vinorelbine and epirubicin stimulate neurite outgrowth of cerebellar neurons via the neural cell adhesion molecule, via myristoylated alanine-rich C kinase substrate, and via fibroblast growth factor receptor, signaling through Erk pathways. Epirubicin 16-26 myristoylated alanine rich protein kinase C substrate Homo sapiens 120-165 26443186-9 2016 Ablating NCAM, inhibiting fibroblast growth factor (FGFR) receptor, or adding the effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) minimize the vinorelbine and epirubicin effects, indicating that they are true PSA mimetics triggering PSA-mediated functions. Vinorelbine 169-180 myristoylated alanine rich protein kinase C substrate Homo sapiens 101-146 26443186-9 2016 Ablating NCAM, inhibiting fibroblast growth factor (FGFR) receptor, or adding the effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) minimize the vinorelbine and epirubicin effects, indicating that they are true PSA mimetics triggering PSA-mediated functions. Vinorelbine 169-180 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-154 26443186-9 2016 Ablating NCAM, inhibiting fibroblast growth factor (FGFR) receptor, or adding the effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) minimize the vinorelbine and epirubicin effects, indicating that they are true PSA mimetics triggering PSA-mediated functions. Epirubicin 185-195 myristoylated alanine rich protein kinase C substrate Homo sapiens 101-146 26443186-9 2016 Ablating NCAM, inhibiting fibroblast growth factor (FGFR) receptor, or adding the effector domain of myristoylated alanine-rich C kinase substrate (MARCKS) minimize the vinorelbine and epirubicin effects, indicating that they are true PSA mimetics triggering PSA-mediated functions. Epirubicin 185-195 myristoylated alanine rich protein kinase C substrate Homo sapiens 148-154 25502213-11 2015 Additionally, we demonstrated an association between CX3CR1 expression and apoptosis prevention by soluble fractalkine (sCX3CL1) in Mos, DCs and MACs. scx3cl1 120-127 myristoylated alanine rich protein kinase C substrate Homo sapiens 145-149 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 101-141 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 143-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-44 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 143-147 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 213-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-44 26470026-7 2015 We also found that over-expression of MARCKS-WT resulted in a significant increase in total cellular phosphatidyl-inositol (4,5) bisphosphate (PIP2) levels, consistent with prior evidence that MARCKS can regulate PIP2 levels. Phosphatidylinositol 4,5-Diphosphate 213-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 193-199 26470026-8 2015 We also found increased staining for PIP2 in the nucleus with MARCKS-WT over-expression compared to MARCKS DeltaED by immunofluorescence. Phosphatidylinositol 4,5-Diphosphate 37-41 myristoylated alanine rich protein kinase C substrate Homo sapiens 62-68 26450120-7 2015 MARCKS knockdown significantly decreased membrane-associated phosphatidylinositol 4,5-bisphosphate (PIP2) levels. Phosphatidylinositol 4,5-Diphosphate 61-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 26450120-7 2015 MARCKS knockdown significantly decreased membrane-associated phosphatidylinositol 4,5-bisphosphate (PIP2) levels. Phosphatidylinositol 4,5-Diphosphate 100-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 26450120-8 2015 Cotransfection with an intact, unphosphorylated MARCKS, which has a high binding affinity for PIP2, restored membrane-associated PIP2 levels and was indispensable for activation of Rac1 and Cdc42 and, ultimately, VSMC migration. Phosphatidylinositol 4,5-Diphosphate 94-98 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 26450120-8 2015 Cotransfection with an intact, unphosphorylated MARCKS, which has a high binding affinity for PIP2, restored membrane-associated PIP2 levels and was indispensable for activation of Rac1 and Cdc42 and, ultimately, VSMC migration. Phosphatidylinositol 4,5-Diphosphate 129-133 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 26450120-8 2015 Cotransfection with an intact, unphosphorylated MARCKS, which has a high binding affinity for PIP2, restored membrane-associated PIP2 levels and was indispensable for activation of Rac1 and Cdc42 and, ultimately, VSMC migration. vsmc 213-217 myristoylated alanine rich protein kinase C substrate Homo sapiens 48-54 26450120-9 2015 Overexpression of MARCKS in differentiated VSMCs increased membrane PIP2 abundance, Rac1 and Cdc42 activity, and cell motility. Phosphatidylinositol 4,5-Diphosphate 68-72 myristoylated alanine rich protein kinase C substrate Homo sapiens 18-24 26450120-13 2015 These effects are mediated by MARCKS sequestering PIP2 at the plasma membrane. Phosphatidylinositol 4,5-Diphosphate 50-54 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-36 26136560-2 2015 In turn, myristoylated alanine-rich C kinase substrate (MARCKS) protein or MARCKS-like protein 1 (MLP-1) at the plasma membrane regulates the delivery of PIP2 to ENaC. Phosphatidylinositol 4,5-Diphosphate 154-158 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-54 26136560-3 2015 MARCKS and MLP-1 are regulated by changes in cytosolic calcium; increasing calcium promotes dissociation of MARCKS from the membrane, but the calcium-regulatory mechanisms are unclear. Calcium 55-62 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-6 26136560-3 2015 MARCKS and MLP-1 are regulated by changes in cytosolic calcium; increasing calcium promotes dissociation of MARCKS from the membrane, but the calcium-regulatory mechanisms are unclear. Calcium 75-82 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 26136560-2 2015 In turn, myristoylated alanine-rich C kinase substrate (MARCKS) protein or MARCKS-like protein 1 (MLP-1) at the plasma membrane regulates the delivery of PIP2 to ENaC. Phosphatidylinositol 4,5-Diphosphate 154-158 myristoylated alanine rich protein kinase C substrate Homo sapiens 56-62 26136560-3 2015 MARCKS and MLP-1 are regulated by changes in cytosolic calcium; increasing calcium promotes dissociation of MARCKS from the membrane, but the calcium-regulatory mechanisms are unclear. Calcium 75-82 myristoylated alanine rich protein kinase C substrate Homo sapiens 108-114 26136560-4 2015 However, it is known that increased intracellular calcium can activate calmodulin and we show that inhibition of calmodulin with calmidazolium increases ENaC activity presumably by regulating MARCKS and MLP-1. calmidazolium 129-142 myristoylated alanine rich protein kinase C substrate Homo sapiens 192-198 26015406-6 2015 We further show that phospho-MARCKS acted upstream of Src activation upon paclitaxel exposure. Paclitaxel 74-84 myristoylated alanine rich protein kinase C substrate Homo sapiens 29-35 25851418-5 2015 Here, we demonstrate that D-MARCKS-ED, composed by unnatural D-amino acids, has the same activities as its enantiomer, L-MARCKS-ED, as a curvature and lipid sensor. d-amino acids 61-74 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 26015406-0 2015 Elevated MARCKS phosphorylation contributes to unresponsiveness of breast cancer to paclitaxel treatment. Paclitaxel 84-94 myristoylated alanine rich protein kinase C substrate Homo sapiens 9-15 26015406-7 2015 Reduction of phospho-MARCKS by knockdown of MARCKS or pharmacological agents increased paclitaxel sensitivity. Paclitaxel 87-97 myristoylated alanine rich protein kinase C substrate Homo sapiens 21-27 26015406-5 2015 Among chemotherapeutic agents, mitotic inhibitors, including paclitaxel, vincristine or eribulin, notably promoted phospho-MARCKS accumulation in multiple breast cancer cells. Paclitaxel 61-71 myristoylated alanine rich protein kinase C substrate Homo sapiens 123-129 26015406-7 2015 Reduction of phospho-MARCKS by knockdown of MARCKS or pharmacological agents increased paclitaxel sensitivity. Paclitaxel 87-97 myristoylated alanine rich protein kinase C substrate Homo sapiens 44-50 26015406-5 2015 Among chemotherapeutic agents, mitotic inhibitors, including paclitaxel, vincristine or eribulin, notably promoted phospho-MARCKS accumulation in multiple breast cancer cells. Vincristine 73-84 myristoylated alanine rich protein kinase C substrate Homo sapiens 123-129 26015406-8 2015 Particularly, a known phospho-MARCKS inhibitor, MANS peptide, was demonstrated to increase paclitaxel efficacy and attenuate angiogenesis/metastasis of xenografted breast cancer cells by decreasing abundance of phospho-MARCKS and messages of inflammatory mediators. Paclitaxel 91-101 myristoylated alanine rich protein kinase C substrate Homo sapiens 30-36 26015406-9 2015 Our data suggest that unresponsiveness of breast cancer to paclitaxel treatment is, at least in part, mediated by phospho-MARCKS and also provide an alternative therapeutic strategy against breast cancer by improving taxanes sensitivity. Paclitaxel 59-69 myristoylated alanine rich protein kinase C substrate Homo sapiens 122-128 25515270-0 2015 In Vitro Neutrophil Migration Requires Protein Kinase C-Delta (delta-PKC)-Mediated Myristoylated Alanine-Rich C-Kinase Substrate (MARCKS) Phosphorylation. Alanine 97-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 130-136 25524703-3 2015 Myristoylated alanine rich C-kinase substrate (MARCKS) is a protein that has the ability to mitigate this signaling cascade by sequestering the target of PI3K, phosphatidylinositol (4,5)-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 160-199 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 25524703-3 2015 Myristoylated alanine rich C-kinase substrate (MARCKS) is a protein that has the ability to mitigate this signaling cascade by sequestering the target of PI3K, phosphatidylinositol (4,5)-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 160-199 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 25524703-3 2015 Myristoylated alanine rich C-kinase substrate (MARCKS) is a protein that has the ability to mitigate this signaling cascade by sequestering the target of PI3K, phosphatidylinositol (4,5)-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 201-205 myristoylated alanine rich protein kinase C substrate Homo sapiens 0-45 25524703-3 2015 Myristoylated alanine rich C-kinase substrate (MARCKS) is a protein that has the ability to mitigate this signaling cascade by sequestering the target of PI3K, phosphatidylinositol (4,5)-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 201-205 myristoylated alanine rich protein kinase C substrate Homo sapiens 47-53 25543853-10 2015 From these results, we concluded that MACs, such as the heterocyclic cyclohexanone analogs in this study, also have potential as MDR reversal agents and may be superior alternatives to the unstable parent compound, CUR. cyclohexanone 69-82 myristoylated alanine rich protein kinase C substrate Homo sapiens 38-42 25757715-10 2015 CONCLUSIONS: MARCKS and PPP1R9A might contribute to spine loss in schizophrenia and bipolar disorder through their interactions, possibly indirect ones, with NMDA signaling pathways that regulate spine structure and function. N-Methylaspartate 158-162 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 25179733-3 2015 We identified selective overexpression of myristoylated alanine-rich C-kinase substrate (MARCKS) in drug-resistant R5 cells. Alanine 56-63 myristoylated alanine rich protein kinase C substrate Homo sapiens 89-95 25179733-5 2015 Functionally, inhibition of MARCKS phosphorylation by enzastaurin or knockdown of the gene by RNAi significantly enhanced the sensitivity of resistant HMCLs and primary MM samples to bortezomib and to other anti-myeloma drugs, providing evidence that MARCKS can modulate drug response. enzastaurin 54-65 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 25179733-5 2015 Functionally, inhibition of MARCKS phosphorylation by enzastaurin or knockdown of the gene by RNAi significantly enhanced the sensitivity of resistant HMCLs and primary MM samples to bortezomib and to other anti-myeloma drugs, providing evidence that MARCKS can modulate drug response. hmcls 151-156 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 25179733-5 2015 Functionally, inhibition of MARCKS phosphorylation by enzastaurin or knockdown of the gene by RNAi significantly enhanced the sensitivity of resistant HMCLs and primary MM samples to bortezomib and to other anti-myeloma drugs, providing evidence that MARCKS can modulate drug response. Bortezomib 183-193 myristoylated alanine rich protein kinase C substrate Homo sapiens 28-34 25179733-8 2015 Importantly, MARCKS knockdown in combination with bortezomib treatment overcame bortezomib resistance, significantly inhibited tumor growth and prolonged host survival in a MM xenograft model. Bortezomib 80-90 myristoylated alanine rich protein kinase C substrate Homo sapiens 13-19 25543853-3 2015 Monocarbonyl analogs of CUR (MACs) are compounds without CUR"s unstable beta-diketone moiety and were reported to have improved stability and in vivo disposition. beta-diketone 72-85 myristoylated alanine rich protein kinase C substrate Homo sapiens 29-33 25543853-5 2015 In this study, we investigated 23 heterocyclic cyclohexanone MACs for inhibitory effects against P-gp, BCRP, MRP1 and MRP5. cyclohexanone 47-60 myristoylated alanine rich protein kinase C substrate Homo sapiens 61-65 25515270-5 2015 We report that treatment of human neutrophils with the delta-PKC inhibitor rottlerin significantly attenuates f-Met-Leu-Phe (fMLF)-induced MARCKS phosphorylation (IC50=5.709 muM), adhesion (IC50=8.4 muM), and migration (IC50=6.7 muM), while alpha-, beta-, and zeta-PKC inhibitors had no significant effect. rottlerin 75-84 myristoylated alanine rich protein kinase C substrate Homo sapiens 139-145 25515270-5 2015 We report that treatment of human neutrophils with the delta-PKC inhibitor rottlerin significantly attenuates f-Met-Leu-Phe (fMLF)-induced MARCKS phosphorylation (IC50=5.709 muM), adhesion (IC50=8.4 muM), and migration (IC50=6.7 muM), while alpha-, beta-, and zeta-PKC inhibitors had no significant effect. N-Formylmethionine Leucyl-Phenylalanine 110-123 myristoylated alanine rich protein kinase C substrate Homo sapiens 139-145 25515270-5 2015 We report that treatment of human neutrophils with the delta-PKC inhibitor rottlerin significantly attenuates f-Met-Leu-Phe (fMLF)-induced MARCKS phosphorylation (IC50=5.709 muM), adhesion (IC50=8.4 muM), and migration (IC50=6.7 muM), while alpha-, beta-, and zeta-PKC inhibitors had no significant effect. N-Formylmethionine Leucyl-Phenylalanine 125-129 myristoylated alanine rich protein kinase C substrate Homo sapiens 139-145 24835554-3 2014 Exposure to MeHg induced a decrease in cell viability of SH-SY5Y cells, which was accompanied by a significant increase in phosphorylation and a reduction in MARCKS expression. mehg 12-16 myristoylated alanine rich protein kinase C substrate Homo sapiens 158-164 24662485-4 2014 We found that the GTP-locked active form of Rab10 binds to membrane-associated MARCKS, whose affinity depends on the phosphorylation status of the MARCKS effector domain. Guanosine Triphosphate 18-21 myristoylated alanine rich protein kinase C substrate Homo sapiens 79-85 24662485-4 2014 We found that the GTP-locked active form of Rab10 binds to membrane-associated MARCKS, whose affinity depends on the phosphorylation status of the MARCKS effector domain. Guanosine Triphosphate 18-21 myristoylated alanine rich protein kinase C substrate Homo sapiens 147-153 25195712-6 2014 An atomistic molecular dynamics (MD) simulation suggested an important role played by the insertion of the Phe residues within MARCKS-ED. Phenylalanine 107-110 myristoylated alanine rich protein kinase C substrate Homo sapiens 127-133 25318062-8 2014 Using shRNA silencing and ectopic expression of wild-type and PSD-mutated (S159/163A) MARCKS, we showed that elevated phospho-MARCKS promoted cancer growth and erlotinib resistance. Erlotinib Hydrochloride 160-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 86-92 25318062-8 2014 Using shRNA silencing and ectopic expression of wild-type and PSD-mutated (S159/163A) MARCKS, we showed that elevated phospho-MARCKS promoted cancer growth and erlotinib resistance. Erlotinib Hydrochloride 160-169 myristoylated alanine rich protein kinase C substrate Homo sapiens 126-132 25318062-10 2014 Interestingly, phospho-MARCKS acted in parallel with increased phosphatidylinositol (3,4,5)-triphosphate pools and AKT activation in cells. phosphatidylinositol 3,4,5-triphosphate 63-104 myristoylated alanine rich protein kinase C substrate Homo sapiens 23-29 25318062-11 2014 Through treatment with a 25-mer peptide targeting the MARCKS PSD motif (MPS peptide), we were able to suppress tumor growth and metastasis in vivo, and reduced levels of phospho-MARCKS, phosphatidylinositol (3,4,5)-triphosphate, and AKT activity. phosphatidylinositol 3,4,5-triphosphate 186-227 myristoylated alanine rich protein kinase C substrate Homo sapiens 54-60 25170921-14 2014 Four (ARRB2, STX1A, TFRC and MARCKS) out of the 37 markers were found to be associated with several neurotransmitters including dopamine. Dopamine 128-136 myristoylated alanine rich protein kinase C substrate Homo sapiens 29-35 24744737-8 2014 Moreover, TPA induced the phosphorylation of MARCKS, which is a membrane-substrate of PKC, resulting in the translocation of phosphorylated MARCKS to the perinuclear region, suggesting that TPA induces macropinocytosis via gammaPKC activation. Tetradecanoylphorbol Acetate 10-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-51 24744737-8 2014 Moreover, TPA induced the phosphorylation of MARCKS, which is a membrane-substrate of PKC, resulting in the translocation of phosphorylated MARCKS to the perinuclear region, suggesting that TPA induces macropinocytosis via gammaPKC activation. Tetradecanoylphorbol Acetate 10-13 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-146 24744737-8 2014 Moreover, TPA induced the phosphorylation of MARCKS, which is a membrane-substrate of PKC, resulting in the translocation of phosphorylated MARCKS to the perinuclear region, suggesting that TPA induces macropinocytosis via gammaPKC activation. Tetradecanoylphorbol Acetate 190-193 myristoylated alanine rich protein kinase C substrate Homo sapiens 45-51 24744737-8 2014 Moreover, TPA induced the phosphorylation of MARCKS, which is a membrane-substrate of PKC, resulting in the translocation of phosphorylated MARCKS to the perinuclear region, suggesting that TPA induces macropinocytosis via gammaPKC activation. Tetradecanoylphorbol Acetate 190-193 myristoylated alanine rich protein kinase C substrate Homo sapiens 140-146 24550450-4 2014 We found that ADP-dependent phosphorylation of key endothelial signaling proteins--including endothelial nitric oxide synthase, AMP-activated protein kinase, and the actin-binding MARCKS protein--was blocked by preincubation with PEG-catalase, which degrades H2O2. Adenosine Diphosphate 14-17 myristoylated alanine rich protein kinase C substrate Homo sapiens 180-186 25051736-2 2014 In spite of the correspondence of the content of abiotic heavy metals to their MACs in the environment, the concentration of lead and cadmium in the internal environment of the organism in 1,6-15,4 times was found to exceed physiological norms that accompanied by a significant deficiency of essential trace elements. Cadmium 134-141 myristoylated alanine rich protein kinase C substrate Homo sapiens 79-83