PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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. Phosphatidylinositol 4,5-Diphosphate 39-43 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. 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 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 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 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 15041659-6 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 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 12670959-1 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 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 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 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 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 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 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 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 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 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 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 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 8824266-6 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 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 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 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 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 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 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 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 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 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 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 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 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 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 26450120-9 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 56-62 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 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 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 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. 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 23704996-13 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 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 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