PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16236797-0 2006 Specific translocation of protein kinase Calpha to the plasma membrane requires both Ca2+ and PIP2 recognition by its C2 domain. Phosphatidylinositol 4,5-Diphosphate 94-98 protein kinase C alpha Homo sapiens 26-47 16310216-4 2006 Phosphorylation results in reduced PKCalpha activity by inhibiting PtdIns(4,5)P2-dependent oligomerization of the syndecan-4 cytoplasmic domain. Phosphatidylinositol 4,5-Diphosphate 67-80 protein kinase C alpha Homo sapiens 35-43 16236797-3 2006 We find that Ca2+-activated PKCalpha and its isolated C2 domain localize exclusively to the plasma membrane in vivo and that a plasma membrane lipid, phosphatidylinositol-4,5-bisphosphate (PIP2), dramatically enhances the Ca2+-triggered binding of the C2 domain to membranes in vitro. Phosphatidylinositol 4,5-Diphosphate 189-193 protein kinase C alpha Homo sapiens 28-36 16236797-4 2006 Similarly, a hybrid construct substituting the PKCalpha Ca2+-binding loops (CBLs) and PIP2 binding site (beta-strands 3-4) into a different C2 domain exhibits native Ca2+-triggered targeting to plasma membrane and recognizes PIP2. Phosphatidylinositol 4,5-Diphosphate 86-90 protein kinase C alpha Homo sapiens 47-55 16236797-4 2006 Similarly, a hybrid construct substituting the PKCalpha Ca2+-binding loops (CBLs) and PIP2 binding site (beta-strands 3-4) into a different C2 domain exhibits native Ca2+-triggered targeting to plasma membrane and recognizes PIP2. Phosphatidylinositol 4,5-Diphosphate 225-229 protein kinase C alpha Homo sapiens 47-55 9553124-5 1998 Data from in vitro kinase assays using purified PKCalpha beta gamma show that in the absence of phosphatidylserine and diolein, PIP2 increased the extent of autophosphorylation of PKCalpha beta gamma and partially activated it to phosphorylate both histone III-S and an epidermal growth factor receptor peptide. Phosphatidylinositol 4,5-Diphosphate 128-132 protein kinase C alpha Homo sapiens 48-56 16114872-5 2005 However, atRA had a biphasic effect on PKCalpha activity in the presence of activating phospholipids, such as phosphatidylserine and phosphatidylinositol 4,5-bisphosphate, yielding activation at low concentrations but inactivation at higher ones. Phosphatidylinositol 4,5-Diphosphate 133-170 protein kinase C alpha Homo sapiens 39-47 11916978-5 2002 Syndecan-4/PIP(2)-dependent PKCalpha activity was significantly increased in PKCdelta DN cells, while PKCdelta overexpression was accompanied by decreased PKCalpha activity. Phosphatidylinositol 4,5-Diphosphate 11-17 protein kinase C alpha Homo sapiens 28-36 9748216-6 1998 The cytoplasmic tail of syndecan-4 is known to undergo multimerization and to activate protein kinase Calpha (PKCalpha), with both events depending on the presence of the commonly occurring phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 242-246 protein kinase C alpha Homo sapiens 110-118 9748216-11 1998 We conclude that Ser183 phosphorylation regulates syndecan-4-dependent activation of PKCalpha by reducing the affinity to PIP2 and inhibiting the oligomerization of syndecan-4 cytoplasmic tails. Phosphatidylinositol 4,5-Diphosphate 122-126 protein kinase C alpha Homo sapiens 85-93 9811229-3 1998 Some cytokines induce PKC activation by stimulating phospholipase C that hydrolyzes phosphatidylinositol bisphosphate (PIP2) into IP3 (intracellular calcium mobilizer) and DAG. Phosphatidylinositol 4,5-Diphosphate 119-123 protein kinase C alpha Homo sapiens 22-25 14645664-6 2003 However, phosphatidylinositol-4,5-bisphosphate PIP2, a lipid ligand for some PH domains, reconstitutes phorbol 12,13-dibutyrate (PDBu) binding to PKD similarly as it does to PKC-alpha and -delta, implying that the PH domain in PKD may not preferentially interact with PIP2. Phosphatidylinositol 4,5-Diphosphate 47-51 protein kinase C alpha Homo sapiens 174-194 9553124-5 1998 Data from in vitro kinase assays using purified PKCalpha beta gamma show that in the absence of phosphatidylserine and diolein, PIP2 increased the extent of autophosphorylation of PKCalpha beta gamma and partially activated it to phosphorylate both histone III-S and an epidermal growth factor receptor peptide. Phosphatidylinositol 4,5-Diphosphate 128-132 protein kinase C alpha Homo sapiens 180-188 9553124-7 1998 Addition of the cytoplasmic syndecan-4 peptide, but not equivalent syndecan-1 or syndecan-2 peptides, potentiated the partial activation of PKCalpha beta gamma by PIP2, resulting in activity greater than that observed with phosphatidylserine, diolein, and calcium. Phosphatidylinositol 4,5-Diphosphate 163-167 protein kinase C alpha Homo sapiens 140-148 8670170-12 1996 These results indicate that, in SH-SY5Y cells, PDBu activation of PKC preferentially inhibits rapid muscarinic receptor-mediated phosphoinositide and Ca2+ responses via suppression of PtdIns(4,5)P2 hydrolysis. Phosphatidylinositol 4,5-Diphosphate 184-197 protein kinase C alpha Homo sapiens 66-69 8626786-10 1996 The PKC-mediated PLD activation was completely inhibited by neomycin, a high affinity ligand for PIP2, and this suppression was recovered by the addition of exogenous PIP2. Phosphatidylinositol 4,5-Diphosphate 97-101 protein kinase C alpha Homo sapiens 4-7 8626786-10 1996 The PKC-mediated PLD activation was completely inhibited by neomycin, a high affinity ligand for PIP2, and this suppression was recovered by the addition of exogenous PIP2. Phosphatidylinositol 4,5-Diphosphate 167-171 protein kinase C alpha Homo sapiens 4-7 8626786-11 1996 Thus, these results suggest that PIP2 is supposed to play a key role in PKC-mediated PLD activity in HL60 membranes. Phosphatidylinositol 4,5-Diphosphate 33-37 protein kinase C alpha Homo sapiens 72-75 24763383-0 2014 Phosphatidylinositol-4,5-bisphosphate enhances anionic lipid demixing by the C2 domain of PKCalpha. Phosphatidylinositol 4,5-Diphosphate 0-37 protein kinase C alpha Homo sapiens 90-98 27706148-6 2016 HomoFRET between full-length PKCalpha molecules is observed when in solution with both calcium and liposomes containing either diacylglycerol (DAG) or phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). Phosphatidylinositol 4,5-Diphosphate 151-188 protein kinase C alpha Homo sapiens 29-37 8387275-0 1993 Activation of purified human protein kinase C alpha and beta I isoenzymes in vitro by Ca2+, phosphatidylinositol and phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 117-154 protein kinase C alpha Homo sapiens 29-51 8387275-9 1993 Replacement of either DAG or PS by phosphatidylglycerol, cardiolipin, phosphatidylcholine and several phosphoinositides revealed that PtdIns(4,5)P2 can act as a PKC activator similar to DAG, whereas PtdIns can substitute for PS as a cofactor of activation. Phosphatidylinositol 4,5-Diphosphate 134-147 protein kinase C alpha Homo sapiens 161-164 8387275-10 1993 Thus, at least for the PKC isoenzymes alpha and beta I, a combination of PtdIns and PtdIns(4,5)P2 can fully replace PS and DAG in vitro as the classical activators of PKC. Phosphatidylinositol 4,5-Diphosphate 84-97 protein kinase C alpha Homo sapiens 23-26 33026061-0 2020 A metabolic reaction-diffusion model for PKCalpha translocation via PIP2 hydrolysis in an endothelial cell. Phosphatidylinositol 4,5-Diphosphate 68-72 protein kinase C alpha Homo sapiens 41-49 33026061-3 2020 In this study, we developed a metabolic reaction-diffusion framework to simulate PKCalpha translocation via PIP2 hydrolysis in an endothelial cell. Phosphatidylinositol 4,5-Diphosphate 108-112 protein kinase C alpha Homo sapiens 81-89 24763383-5 2014 The demixing induced by the C2alpha domain may have a physiological significance since it means that the binding of PKCalpha to membranes is accompanied by the formation of domains enriched in activating lipids, like phosphatidylserine and PIP2. Phosphatidylinositol 4,5-Diphosphate 240-244 protein kinase C alpha Homo sapiens 116-124 21044681-5 2011 Our findings reveal that PKCalpha can rescue the removal or masking of PtdIns(4,5)P2, indicating that the inositol lipid is upstream of PKC. Phosphatidylinositol 4,5-Diphosphate 71-84 protein kinase C alpha Homo sapiens 25-33 21144818-2 2011 We have used attenuated total internal reflection infrared spectroscopy (ATR-IR) spectroscopy to study the association of the C2 domain from protein kinase Calpha (PKCalpha) with different phospholipid membranes, so as to characterise the mode of membrane docking and its modulation by the second-messenger lipid PIP2. Phosphatidylinositol 4,5-Diphosphate 313-317 protein kinase C alpha Homo sapiens 164-172 21144818-7 2011 In the process of membrane docking, the tilt angle increases to alpha=44 in the presence of PIP2, indicating that the beta-sandwich comes closer to the membrane surface, so confirming the importance of this lipid in determining docking of the C2 domain and consequent activation of PKCalpha. Phosphatidylinositol 4,5-Diphosphate 93-97 protein kinase C alpha Homo sapiens 283-291 21044681-5 2011 Our findings reveal that PKCalpha can rescue the removal or masking of PtdIns(4,5)P2, indicating that the inositol lipid is upstream of PKC. Phosphatidylinositol 4,5-Diphosphate 71-84 protein kinase C alpha Homo sapiens 25-28 19346474-0 2009 Structural and mechanistic insights into the association of PKCalpha-C2 domain to PtdIns(4,5)P2. Phosphatidylinositol 4,5-Diphosphate 82-95 protein kinase C alpha Homo sapiens 60-68 17367165-6 2007 For the isolated PKCalpha C2 domain in the presence of physiological Ca2+ levels, the target lipids phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) are together sufficient to recruit the PKCalpha C2 domain to a lipid mixture mimicking the plasma membrane inner leaflet. Phosphatidylinositol 4,5-Diphosphate 128-165 protein kinase C alpha Homo sapiens 17-25 17367165-6 2007 For the isolated PKCalpha C2 domain in the presence of physiological Ca2+ levels, the target lipids phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) are together sufficient to recruit the PKCalpha C2 domain to a lipid mixture mimicking the plasma membrane inner leaflet. Phosphatidylinositol 4,5-Diphosphate 128-165 protein kinase C alpha Homo sapiens 212-220 17367165-6 2007 For the isolated PKCalpha C2 domain in the presence of physiological Ca2+ levels, the target lipids phosphatidylserine (PS) and phosphatidylinositol-4,5-bisphosphate (PIP2) are together sufficient to recruit the PKCalpha C2 domain to a lipid mixture mimicking the plasma membrane inner leaflet. Phosphatidylinositol 4,5-Diphosphate 167-171 protein kinase C alpha Homo sapiens 17-25