PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23909401-0 2013 Collaboration of AMPK and PKC to induce phosphorylation of Ser413 on PIP5K1B resulting in decreased kinase activity and reduced PtdIns(4,5)P2 synthesis in response to oxidative stress and energy restriction. Phosphatidylinositol 4,5-Diphosphate 128-141 proline rich transmembrane protein 2 Homo sapiens 26-29 24560147-4 2014 Gq protein-coupled receptors of the plasma membrane activate phospholipase C (PLC) which cleaves the minor plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into the second messengers diacylgycerol and inositol 1,4,5-trisphosphate, leading to calcium release, protein kinase C (PKC) activation, and PI(4,5)P2 depletion. Phosphatidylinositol 4,5-Diphosphate 129-166 proline rich transmembrane protein 2 Homo sapiens 282-298 24560147-4 2014 Gq protein-coupled receptors of the plasma membrane activate phospholipase C (PLC) which cleaves the minor plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into the second messengers diacylgycerol and inositol 1,4,5-trisphosphate, leading to calcium release, protein kinase C (PKC) activation, and PI(4,5)P2 depletion. Phosphatidylinositol 4,5-Diphosphate 129-166 proline rich transmembrane protein 2 Homo sapiens 300-303 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 proline rich transmembrane protein 2 Homo sapiens 24-27 27119641-8 2016 More broadly, the Ca(2+)-PKC-stimulated release of free PIP2 may well regulate the membrane association of other PIP2-binding proteins, and the findings illustrate the power of single-molecule analysis to elucidate key dynamic and mechanistic features of multiprotein signaling pathways on membrane surfaces. Phosphatidylinositol 4,5-Diphosphate 56-60 proline rich transmembrane protein 2 Homo sapiens 25-28 27119641-8 2016 More broadly, the Ca(2+)-PKC-stimulated release of free PIP2 may well regulate the membrane association of other PIP2-binding proteins, and the findings illustrate the power of single-molecule analysis to elucidate key dynamic and mechanistic features of multiprotein signaling pathways on membrane surfaces. Phosphatidylinositol 4,5-Diphosphate 113-117 proline rich transmembrane protein 2 Homo sapiens 25-28 23909401-10 2013 Our studies show that collaboration between AMPK and PKC dictates the extent of Ser413 phosphorylation on PIP5K1B and regulates PtdIns(4,5)P2 synthesis. Phosphatidylinositol 4,5-Diphosphate 128-141 proline rich transmembrane protein 2 Homo sapiens 53-56 10395936-7 1999 Since PMXB-insensitive PKC exerts a stimulatory effect on PtdIns-4,5-P2-PLC production, this original mechanism may be considered as a new signalling pathway under control of PKC. Phosphatidylinositol 4,5-Diphosphate 58-71 proline rich transmembrane protein 2 Homo sapiens 23-26 22609963-0 2012 Diacylglycerol stimulates acrosomal exocytosis by feeding into a PKC- and PLD1-dependent positive loop that continuously supplies phosphatidylinositol 4,5-bisphosphate. Phosphatidylinositol 4,5-Diphosphate 130-167 proline rich transmembrane protein 2 Homo sapiens 65-68 10395936-3 1999 A 15-min pre-treatment with polymyxin B (PMXB), a protein kinase C (PKC) inhibitor acting at the phosphatidylserine (PS) binding site, suppressed PDBu stimulatory effects on free calcium entry and fluid resorption but not on phosphatidylinositol 4, 5-bisphosphate (PtdIns-4,5-P2) breakdown. Phosphatidylinositol 4,5-Diphosphate 225-263 proline rich transmembrane protein 2 Homo sapiens 68-71 10395936-3 1999 A 15-min pre-treatment with polymyxin B (PMXB), a protein kinase C (PKC) inhibitor acting at the phosphatidylserine (PS) binding site, suppressed PDBu stimulatory effects on free calcium entry and fluid resorption but not on phosphatidylinositol 4, 5-bisphosphate (PtdIns-4,5-P2) breakdown. Phosphatidylinositol 4,5-Diphosphate 265-278 proline rich transmembrane protein 2 Homo sapiens 68-71 18690019-6 2007 We show that the PKC-induced effects strongly depend on PIP2 levels in the membrane. Phosphatidylinositol 4,5-Diphosphate 56-60 proline rich transmembrane protein 2 Homo sapiens 17-20 18690019-7 2007 At the same time, we show that PKC destabilizes Kir3/PIP2 interactions and enhances the effects of PIP2 depletion on channel activity. Phosphatidylinositol 4,5-Diphosphate 53-57 proline rich transmembrane protein 2 Homo sapiens 31-34 18690019-10 2007 We also show that stabilization of Kir3/PIP2 interactions by Gbetagamma attenuates both PKC and Gq-mediated current inhibition, suggesting that diverse pathways regulate Kir3 activity through modulation of channel interactions with PIP2. Phosphatidylinositol 4,5-Diphosphate 40-44 proline rich transmembrane protein 2 Homo sapiens 88-91 10395936-7 1999 Since PMXB-insensitive PKC exerts a stimulatory effect on PtdIns-4,5-P2-PLC production, this original mechanism may be considered as a new signalling pathway under control of PKC. Phosphatidylinositol 4,5-Diphosphate 58-71 proline rich transmembrane protein 2 Homo sapiens 175-178 9237245-9 1997 The products of phosphatidyl-inositol bisphosphate (PIP2) hydrolysis by PLC diacylglycerol (DAG) and inositol-trisphosphate (IP3) will lead to PKC translocation to the plasma membrane and its activation. Phosphatidylinositol 4,5-Diphosphate 52-56 proline rich transmembrane protein 2 Homo sapiens 143-146 9148913-6 1997 Unlike other tested phospholipids, phosphatidylinositol 4,5-bisphosphate, which binds to several PH domains, competed with PKC for binding to the PH domain apparently because their binding sites on the amino-terminal portion of the PH domains overlap. Phosphatidylinositol 4,5-Diphosphate 35-72 proline rich transmembrane protein 2 Homo sapiens 123-126 9148913-14 1997 These results indicate that PKC binding to PH domains involve the beta2-beta3 region of the Btk PH domain and the C1 region of PKC, and agents that interact with either of these regions (i.e. phosphatidylinositol 4,5-bisphosphate binding to the PH domain and PMA binding to the C1 region of PKC) might act to regulate PKC-PH domain binding. Phosphatidylinositol 4,5-Diphosphate 192-229 proline rich transmembrane protein 2 Homo sapiens 28-31 35588786-0 2022 Protein Kinase C regulation of ion channels: the involvement of PIP2. Phosphatidylinositol 4,5-Diphosphate 64-68 proline rich transmembrane protein 2 Homo sapiens 0-16 8613911-7 1996 Hydrolysis of PIP2 by PIP2-specific phospholipase C produces equimolar amounts of inositol 1,4,5-triphosphate and diacylglycerol, which may interact synergistically to activate PKC and develop tone. Phosphatidylinositol 4,5-Diphosphate 14-18 proline rich transmembrane protein 2 Homo sapiens 177-180 8613911-7 1996 Hydrolysis of PIP2 by PIP2-specific phospholipase C produces equimolar amounts of inositol 1,4,5-triphosphate and diacylglycerol, which may interact synergistically to activate PKC and develop tone. Phosphatidylinositol 4,5-Diphosphate 22-26 proline rich transmembrane protein 2 Homo sapiens 177-180 7917792-1 1994 Phosphatidylinositol 4,5-bisphosphate (PIP2) activates protein kinase C (PKC) in the presence of phosphatidylserine and calcium. Phosphatidylinositol 4,5-Diphosphate 0-37 proline rich transmembrane protein 2 Homo sapiens 55-71 7917792-1 1994 Phosphatidylinositol 4,5-bisphosphate (PIP2) activates protein kinase C (PKC) in the presence of phosphatidylserine and calcium. Phosphatidylinositol 4,5-Diphosphate 0-37 proline rich transmembrane protein 2 Homo sapiens 73-76 7917792-1 1994 Phosphatidylinositol 4,5-bisphosphate (PIP2) activates protein kinase C (PKC) in the presence of phosphatidylserine and calcium. Phosphatidylinositol 4,5-Diphosphate 39-43 proline rich transmembrane protein 2 Homo sapiens 55-71 7917792-1 1994 Phosphatidylinositol 4,5-bisphosphate (PIP2) activates protein kinase C (PKC) in the presence of phosphatidylserine and calcium. Phosphatidylinositol 4,5-Diphosphate 39-43 proline rich transmembrane protein 2 Homo sapiens 73-76 7917792-2 1994 Recently it has been demonstrated that direct interaction of PKC with PIP2 in the absence of divalent cation inactivates this kinase. Phosphatidylinositol 4,5-Diphosphate 70-74 proline rich transmembrane protein 2 Homo sapiens 61-64 7917792-5 1994 All the phosphoinositides: PIP2, phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol (PI) inactivated PKC with an IC50 of 0.4 microM for PIP2, 5 microM for PIP and 10 microM for PI. Phosphatidylinositol 4,5-Diphosphate 27-31 proline rich transmembrane protein 2 Homo sapiens 114-117 7917792-5 1994 All the phosphoinositides: PIP2, phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol (PI) inactivated PKC with an IC50 of 0.4 microM for PIP2, 5 microM for PIP and 10 microM for PI. Phosphatidylinositol 4,5-Diphosphate 149-153 proline rich transmembrane protein 2 Homo sapiens 114-117 7917792-7 1994 Time-dependent studies showed very rapid inactivation of PKC by PIP2. Phosphatidylinositol 4,5-Diphosphate 64-68 proline rich transmembrane protein 2 Homo sapiens 57-60 1850993-1 1991 Phosphatidylinositol 4,5-bisphosphate (PIP2) as well as diacylglycerol (DG) activate protein kinase C (PKC) in the presence of calcium and phosphatidylserine. Phosphatidylinositol 4,5-Diphosphate 0-37 proline rich transmembrane protein 2 Homo sapiens 103-106 1850993-1 1991 Phosphatidylinositol 4,5-bisphosphate (PIP2) as well as diacylglycerol (DG) activate protein kinase C (PKC) in the presence of calcium and phosphatidylserine. Phosphatidylinositol 4,5-Diphosphate 39-43 proline rich transmembrane protein 2 Homo sapiens 103-106 1850993-9 1991 A PIP2 analog in which inositol carbons 2-4 and the 4-phosphate have been removed, 1-phosphatidyl-rac-glycerol-3-phosphate (PGP), is completely inactive as PKC effector; this suggests that both 4-and 5-phosphate are engaged in the PIP2(5-).Ca.PKC complex. Phosphatidylinositol 4,5-Diphosphate 2-6 proline rich transmembrane protein 2 Homo sapiens 243-246 2826275-8 1987 Thus PMA and DAG, by a mechanism involving PKC-mediated attenuation of secretagogue-induced hydrolysis of PIP2, decreases IPX production, and therefore PKC activation may exert negative feedback regulation on anterior pituitary secretory activity. Phosphatidylinositol 4,5-Diphosphate 106-110 proline rich transmembrane protein 2 Homo sapiens 43-46 2829877-0 1988 Protein kinase C-dependent phosphorylation of profilin is specifically stimulated by phosphatidylinositol bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 120-124 proline rich transmembrane protein 2 Homo sapiens 0-16 2829877-2 1988 Phosphatidylinositol bisphosphate (PIP2) was an effective activator of the profilin phosphorylation by PKC and caused a maximum 13-fold increase of Vmax with a half maximal effect at 40 micrograms/ml. Phosphatidylinositol 4,5-Diphosphate 35-39 proline rich transmembrane protein 2 Homo sapiens 103-106 2829877-5 1988 It is suggested that PIP2 modifies the nature of the profilin-PKC interactions. Phosphatidylinositol 4,5-Diphosphate 21-25 proline rich transmembrane protein 2 Homo sapiens 62-65