PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27042944-3 2016 When compared to mus long atomistic simulations or previous experimental findings, scFix MARTINI simulations reproduced all key interactions between the well-studied PLC-delta1 pleckstrin homology domain and a phosphatidylinositol-4,5-bisphosphate (PIP2) containing lipid membrane. Phosphatidylinositol 4,5-Diphosphate 210-247 phospholipase C delta 1 Homo sapiens 166-176 27042944-3 2016 When compared to mus long atomistic simulations or previous experimental findings, scFix MARTINI simulations reproduced all key interactions between the well-studied PLC-delta1 pleckstrin homology domain and a phosphatidylinositol-4,5-bisphosphate (PIP2) containing lipid membrane. Phosphatidylinositol 4,5-Diphosphate 249-253 phospholipase C delta 1 Homo sapiens 166-176 26040325-4 2015 Here, we report a method for accurate determination of the binding affinity and specificity between proteins and phospholipids using a model interaction between PLC-delta1/PH and phosphoinositide phospholipid PtdIns(4,5)P2. Phosphatidylinositol 4,5-Diphosphate 209-222 phospholipase C delta 1 Homo sapiens 161-171 26365802-6 2015 In contrast, PtdIns(4,5)P2 binding to the PH domain of PLC delta1 was hyperbolic. Phosphatidylinositol 4,5-Diphosphate 13-26 phospholipase C delta 1 Homo sapiens 55-65 16246104-6 2005 A classic example of the latter is the PH domain of phospholipase Cdelta1, which binds both phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate. Phosphatidylinositol 4,5-Diphosphate 92-129 phospholipase C delta 1 Homo sapiens 52-73 22496355-9 2012 Sequestration of PIP2 by ectopic overexpression of the pleckstrin homology domain of phospholipase C-delta1 protected cells from ATO-induced cell death. Phosphatidylinositol 4,5-Diphosphate 17-21 phospholipase C delta 1 Homo sapiens 85-107 17908156-2 2007 Much of the recent knowledge about it has come from a new technique to visualize PtdIns(4,5)P(2)in vivo, by expressing a green or yellow fluorescent protein (GFP or YFP) fused to the pleckstrin homology (PH) domain of human PLCdelta1 that specifically binds PtdIns(4,5)P(2). Phosphatidylinositol 4,5-Diphosphate 81-96 phospholipase C delta 1 Homo sapiens 224-233 21514270-4 2011 The syntenin-2 postsynaptic density protein/disc large/zona occludens (PDZ) domain and pleckstrin homology domain of phospholipase C-delta1 (PLCdelta1 PHD) possess high affinity for phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2)) mainly localized to the nucleus and plasma membrane, respectively. Phosphatidylinositol 4,5-Diphosphate 182-219 phospholipase C delta 1 Homo sapiens 117-154 10364218-1 1999 We recently cloned a novel signaling molecule, p122, that shows a GTPase-activating activity specific for Rho and the ability to enhance the phosphatidylinositol 4,5-bisphosphate-hydrolyzing activity of phospholipase C delta1 in vitro. Phosphatidylinositol 4,5-Diphosphate 141-178 phospholipase C delta 1 Homo sapiens 203-225 15755258-2 2005 PH-PLCdelta1 binds with high specificity to the headgroup of PtdIns(4,5)P2, but little is known about its interfacial properties. Phosphatidylinositol 4,5-Diphosphate 61-74 phospholipase C delta 1 Homo sapiens 3-12 15755258-3 2005 In the present study, we show that PH-PLCdelta1 is also membrane-active and can insert significantly into PtdIns(4,5)P2-containing monolayers at physiological (bilayer-equivalent) surface pressures. Phosphatidylinositol 4,5-Diphosphate 106-119 phospholipase C delta 1 Homo sapiens 38-47 15755258-5 2005 Whereas the majority of PtdIns(4,5)P2-bound PH-PLCdelta1 can be displaced by adding excess of soluble headgroup [Ins(1,4,5)P3], membrane activity of PH-PLCdelta1 cannot. Phosphatidylinositol 4,5-Diphosphate 24-37 phospholipase C delta 1 Homo sapiens 47-56 15755258-7 2005 Significant monolayer insertion remains when the phosphoinositide-binding site is mutated, and PH-PLCdelta1 can insert into monolayers that contain no PtdIns(4,5)P2 at all. Phosphatidylinositol 4,5-Diphosphate 151-164 phospholipase C delta 1 Homo sapiens 98-107 15755258-8 2005 Our results suggest a model in which reversible membrane binding of PH-PLCdelta1, mediated by PtdIns(4,5)P2 or other acidic phospholipids, occurs without membrane insertion. Phosphatidylinositol 4,5-Diphosphate 94-107 phospholipase C delta 1 Homo sapiens 71-80 15778699-14 2005 Furthermore, internalization was inhibited by the PH domain of phospholipase C-delta1, which sequesters PIP2, and synaptotagmin was now unable to rescue. Phosphatidylinositol 4,5-Diphosphate 104-108 phospholipase C delta 1 Homo sapiens 63-85 15447683-9 2004 Microinjection of the plekstrin homology domain of phospholipase C (PLC)delta1, which binds PIP2, enabled LPA to elicit cell rounding, consistent with a requirement for PIP2 reduction. Phosphatidylinositol 4,5-Diphosphate 92-96 phospholipase C delta 1 Homo sapiens 51-78 15447683-9 2004 Microinjection of the plekstrin homology domain of phospholipase C (PLC)delta1, which binds PIP2, enabled LPA to elicit cell rounding, consistent with a requirement for PIP2 reduction. Phosphatidylinositol 4,5-Diphosphate 169-173 phospholipase C delta 1 Homo sapiens 51-78 11964166-0 2002 Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C delta1. Phosphatidylinositol 4,5-Diphosphate 28-65 phospholipase C delta 1 Homo sapiens 106-128 11325731-3 2001 When a solution containing PLC-delta flows past the bead, the enzyme adsorbs to the surface and hydrolyzes PIP2 to form the neutral lipid diacylglycerol. Phosphatidylinositol 4,5-Diphosphate 107-111 phospholipase C delta 1 Homo sapiens 27-36 11325731-4 2001 We observed a nonexponential decay of PIP2 on the bead with time that is consistent with a model based on the known structural properties of PLC-delta. Phosphatidylinositol 4,5-Diphosphate 38-42 phospholipase C delta 1 Homo sapiens 141-150 10491207-2 1999 The binding to phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] by PLC-delta1 is proposed to be the critical interaction required for membrane localization to where the substrate resides; it is also required for the Ca(2+)-dependent activation of PLC-delta1 observed in the permeabilized cells. Phosphatidylinositol 4,5-Diphosphate 15-52 phospholipase C delta 1 Homo sapiens 72-82 10491207-2 1999 The binding to phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] by PLC-delta1 is proposed to be the critical interaction required for membrane localization to where the substrate resides; it is also required for the Ca(2+)-dependent activation of PLC-delta1 observed in the permeabilized cells. Phosphatidylinositol 4,5-Diphosphate 15-52 phospholipase C delta 1 Homo sapiens 252-262 10491207-2 1999 The binding to phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] by PLC-delta1 is proposed to be the critical interaction required for membrane localization to where the substrate resides; it is also required for the Ca(2+)-dependent activation of PLC-delta1 observed in the permeabilized cells. Phosphatidylinositol 4,5-Diphosphate 54-67 phospholipase C delta 1 Homo sapiens 72-82 10491207-2 1999 The binding to phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] by PLC-delta1 is proposed to be the critical interaction required for membrane localization to where the substrate resides; it is also required for the Ca(2+)-dependent activation of PLC-delta1 observed in the permeabilized cells. Phosphatidylinositol 4,5-Diphosphate 54-67 phospholipase C delta 1 Homo sapiens 252-262 10491207-5 1999 A Ca2+ dependent increase in the binding to PtdIns(4,5)P2 was observed with a full-length PLC-delta1, while the isolated PH domain did not show any Ca2+ dependence. Phosphatidylinositol 4,5-Diphosphate 44-57 phospholipase C delta 1 Homo sapiens 90-100 16000311-8 2005 PLCzeta and the closely related PLCdelta1 had similar K(m) values for phosphatidylinositol 4,5-bisphosphate, but PLCzeta was around 100 times more sensitive to Ca2+ than was PLCdelta1. Phosphatidylinositol 4,5-Diphosphate 70-107 phospholipase C delta 1 Homo sapiens 32-41 15456883-3 2004 Ultrafast-acquisition and superresolution deconvolution microscopy of cultured adipocytes expressing an enhanced green fluorescent protein- or enhanced cyan fluorescent protein (ECFP)-tagged phospholipase Cdelta1 (PLCdelta1) pleckstrin homology (PH) domain reveals that these zones spatially coincide with large-scale PtdIns(4,5)P2-rich plasma membrane patches (PRMPs). Phosphatidylinositol 4,5-Diphosphate 318-331 phospholipase C delta 1 Homo sapiens 191-223 14670369-7 2004 Translocation time courses and efficiencies of the diacylglycerol-sensing PKC epsilon-CFP and the InsP(3)/phosphatidylinositol-4,5-bisphosphate-sensing YFP-PLC-delta 1(PH) were closely correlated. Phosphatidylinositol 4,5-Diphosphate 106-143 phospholipase C delta 1 Homo sapiens 156-167 10419523-2 1999 The rate of PLCdelta1 hydrolysis of phosphatidylinositol 4,5-bisphosphate was stimulated 20-fold by phosphatidylserine (PS), 4-fold by phosphatidic acid (PA), and not at all by phosphatidylethanolamine or phosphatidylcholine (PC). Phosphatidylinositol 4,5-Diphosphate 36-73 phospholipase C delta 1 Homo sapiens 12-21 10364218-6 1999 Using Fluo-3-based Ca2+ microscopy, we found that p122 evoked a rapid elevation of intracellular Ca2+ levels, suggesting that p122 stimulates the phosphatidylinositol 4, 5-bisphosphate-hydrolyzing activity of phospholipase C delta1. Phosphatidylinositol 4,5-Diphosphate 146-184 phospholipase C delta 1 Homo sapiens 209-231 9588182-6 1998 Site-directed mutagenesis of the glutathione-S-transferase (GST)/PLC-delta 1 fusion protein changing Arg105 to His resulted in a fourfold decrease in the affinity of specific Ins(1,4,5)P3 binding and a reduction in PtdIns(4,5)P2 hydrolysing activity to about 40% of that of the wild-type enzyme. Phosphatidylinositol 4,5-Diphosphate 215-228 phospholipase C delta 1 Homo sapiens 65-76 9588182-2 1998 One of the delta-type isoforms, PLC-delta 1, binds to both phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) with a high affinity via its pleckstrin homology (PH) domain. Phosphatidylinositol 4,5-Diphosphate 59-96 phospholipase C delta 1 Homo sapiens 11-43 9588182-2 1998 One of the delta-type isoforms, PLC-delta 1, binds to both phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) with a high affinity via its pleckstrin homology (PH) domain. Phosphatidylinositol 4,5-Diphosphate 98-111 phospholipase C delta 1 Homo sapiens 11-43 9512420-3 1998 Here, we tested this hypothesis by using an in vivo fluorescent indicator for PtdIns(4,5)P2, by tagging the PH domain of phospholipase C delta 1 (PLC-delta 1) with the green fluorescent protein (GFP-PH). Phosphatidylinositol 4,5-Diphosphate 78-91 phospholipase C delta 1 Homo sapiens 121-144 9512420-3 1998 Here, we tested this hypothesis by using an in vivo fluorescent indicator for PtdIns(4,5)P2, by tagging the PH domain of phospholipase C delta 1 (PLC-delta 1) with the green fluorescent protein (GFP-PH). Phosphatidylinositol 4,5-Diphosphate 78-91 phospholipase C delta 1 Homo sapiens 146-157 8387776-4 1993 Binding of 50% of PLC delta occurred at 0.25 nmol/ml PIP2 when LUVs composed of PE + PC (molar ratio of 80:20), plus various amounts of PIP2, were used at a constant phospholipid concentration of 300 nmol/ml. Phosphatidylinositol 4,5-Diphosphate 53-57 phospholipase C delta 1 Homo sapiens 18-27 9417098-1 1998 The pleckstrin homology (PH) domain of phosphatidylinositol-specific phospholipase C-delta1 (PLC-delta1) binds to both D-myo-inositol 1,4, 5-trisphosphate (Ins(1,4,5)P3) and phosphatidylinositol 4, 5-bisphosphate (PtdIns(4,5)P2) with high affinities. Phosphatidylinositol 4,5-Diphosphate 174-212 phospholipase C delta 1 Homo sapiens 69-91 9417098-1 1998 The pleckstrin homology (PH) domain of phosphatidylinositol-specific phospholipase C-delta1 (PLC-delta1) binds to both D-myo-inositol 1,4, 5-trisphosphate (Ins(1,4,5)P3) and phosphatidylinositol 4, 5-bisphosphate (PtdIns(4,5)P2) with high affinities. Phosphatidylinositol 4,5-Diphosphate 174-212 phospholipase C delta 1 Homo sapiens 93-103 9417098-1 1998 The pleckstrin homology (PH) domain of phosphatidylinositol-specific phospholipase C-delta1 (PLC-delta1) binds to both D-myo-inositol 1,4, 5-trisphosphate (Ins(1,4,5)P3) and phosphatidylinositol 4, 5-bisphosphate (PtdIns(4,5)P2) with high affinities. Phosphatidylinositol 4,5-Diphosphate 214-227 phospholipase C delta 1 Homo sapiens 69-91 9417098-1 1998 The pleckstrin homology (PH) domain of phosphatidylinositol-specific phospholipase C-delta1 (PLC-delta1) binds to both D-myo-inositol 1,4, 5-trisphosphate (Ins(1,4,5)P3) and phosphatidylinositol 4, 5-bisphosphate (PtdIns(4,5)P2) with high affinities. Phosphatidylinositol 4,5-Diphosphate 214-227 phospholipase C delta 1 Homo sapiens 93-103 9168154-8 1997 When the activity of PLC delta1 was assayed with PIP2 in the erythrocyte membrane as substrate, sphingosine strongly inhibited PLC delta1. Phosphatidylinositol 4,5-Diphosphate 49-53 phospholipase C delta 1 Homo sapiens 21-31 8942652-1 1996 We measured the ability of sphingomyelin (SPM) to inhibit phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] hydrolysis catalyzed by human phospholipase C-delta 1 (PLC-delta 1) in model membranes and detergent phospholipid mixed micelles. Phosphatidylinositol 4,5-Diphosphate 58-95 phospholipase C delta 1 Homo sapiens 138-161 8798711-0 1996 Positive charge at position 549 is essential for phosphatidylinositol 4,5-bisphosphate-hydrolyzing but not phosphatidylinositol-hydrolyzing activities of human phospholipase C delta1. Phosphatidylinositol 4,5-Diphosphate 49-86 phospholipase C delta 1 Homo sapiens 160-182 8798711-11 1996 Taken together, these results suggest that positive charge at position 549 of PLCdelta1 protein is essential for the enzyme to recognize and catalyze the hydrolysis of PIP2 but not PI. Phosphatidylinositol 4,5-Diphosphate 168-172 phospholipase C delta 1 Homo sapiens 78-87 7890667-5 1995 Phospholipid vesicle binding experiments showed that these three cleavage-defective mutant forms of PLC delta 1 could specifically bind to phosphatidylinositol 4,5-bisphosphate (PIP2) with an affinity similar to that of wild type enzyme. Phosphatidylinositol 4,5-Diphosphate 139-176 phospholipase C delta 1 Homo sapiens 100-111 7890667-5 1995 Phospholipid vesicle binding experiments showed that these three cleavage-defective mutant forms of PLC delta 1 could specifically bind to phosphatidylinositol 4,5-bisphosphate (PIP2) with an affinity similar to that of wild type enzyme. Phosphatidylinositol 4,5-Diphosphate 178-182 phospholipase C delta 1 Homo sapiens 100-111 7890667-6 1995 Western blotting analysis of trypsin-treated enzyme-PIP2 complexes revealed that a 67-kDa major protein fragment survived trypsin digestion if the wild type enzyme, E341G, or H356L mutant PLC delta 1 was preincubated with 7.5 microM PIP2, whereas if it was preincubated with 80 microM PIP2, the size of major protein surviving was comparable to that of intact enzyme. Phosphatidylinositol 4,5-Diphosphate 52-56 phospholipase C delta 1 Homo sapiens 188-199 7890667-8 1995 These observations suggest that PLC delta 1 can recognize PIP2 through a high affinity and a low affinity binding site and that residues Glu341 and His356 are not involved in either high affinity or low affinity PIP2 binding but rather are essential for the Ca(2+)-dependent cleavage activity of PLC. Phosphatidylinositol 4,5-Diphosphate 58-62 phospholipase C delta 1 Homo sapiens 32-43 8810295-0 1996 Phosphatidylinositol 4,5-bisphosphate binding to the pleckstrin homology domain of phospholipase C-delta1 enhances enzyme activity. Phosphatidylinositol 4,5-Diphosphate 0-37 phospholipase C delta 1 Homo sapiens 83-105 8810295-7 1996 When a nested set of PH domain deletions up to 70 amino acids from the N terminus of PLCdelta1 were constructed, the deletion mutant enzymes all catalyzed the hydrolysis of the micelle forms of PI and PIP2 with specific activities comparable with those of the wild type enzyme. Phosphatidylinositol 4,5-Diphosphate 201-205 phospholipase C delta 1 Homo sapiens 85-94 8810295-11 1996 Analysis of PIP2-stimulated PI hydrolysis by a dual substrate binding model of catalysis revealed that the micellar dissociation constant (Ks) of PLCdelta1 for the PI/PS/PC vesicles was reduced from 558 microM to 53 microM, and the interfacial Michaelis constant (Km) was reduced from 0.21 to 0.06 by PIP2. Phosphatidylinositol 4,5-Diphosphate 12-16 phospholipase C delta 1 Homo sapiens 146-155 8810295-11 1996 Analysis of PIP2-stimulated PI hydrolysis by a dual substrate binding model of catalysis revealed that the micellar dissociation constant (Ks) of PLCdelta1 for the PI/PS/PC vesicles was reduced from 558 microM to 53 microM, and the interfacial Michaelis constant (Km) was reduced from 0.21 to 0.06 by PIP2. Phosphatidylinositol 4,5-Diphosphate 301-305 phospholipase C delta 1 Homo sapiens 146-155 8387776-4 1993 Binding of 50% of PLC delta occurred at 0.25 nmol/ml PIP2 when LUVs composed of PE + PC (molar ratio of 80:20), plus various amounts of PIP2, were used at a constant phospholipid concentration of 300 nmol/ml. Phosphatidylinositol 4,5-Diphosphate 136-140 phospholipase C delta 1 Homo sapiens 18-27 8387776-5 1993 When LUVs composed of PE + PC + PIP2 (molar ratio of 79:20:1) were tested as a function of increasing phospholipid concentration, 50% binding of PLC delta occurred at 1.2 nmol/ml PIP2 and 120 nmol/ml total phospholipid. Phosphatidylinositol 4,5-Diphosphate 32-36 phospholipase C delta 1 Homo sapiens 145-154 8387776-7 1993 These showed that 50% binding of PLC delta occurred at a level of 0.9 nmol/ml PIP2 with 80 nmol/ml PC; at 2.2 nmol/ml PIP2 with 170 nmol/ml PS; at 4.2 nmol/ml PIP2 with 320 nmol/ml PI; and at 0.26 nmol/ml PIP2 with 20 nmol/ml total liver phospholipids. Phosphatidylinositol 4,5-Diphosphate 78-82 phospholipase C delta 1 Homo sapiens 33-42 8387776-7 1993 These showed that 50% binding of PLC delta occurred at a level of 0.9 nmol/ml PIP2 with 80 nmol/ml PC; at 2.2 nmol/ml PIP2 with 170 nmol/ml PS; at 4.2 nmol/ml PIP2 with 320 nmol/ml PI; and at 0.26 nmol/ml PIP2 with 20 nmol/ml total liver phospholipids. Phosphatidylinositol 4,5-Diphosphate 118-122 phospholipase C delta 1 Homo sapiens 33-42 8387776-7 1993 These showed that 50% binding of PLC delta occurred at a level of 0.9 nmol/ml PIP2 with 80 nmol/ml PC; at 2.2 nmol/ml PIP2 with 170 nmol/ml PS; at 4.2 nmol/ml PIP2 with 320 nmol/ml PI; and at 0.26 nmol/ml PIP2 with 20 nmol/ml total liver phospholipids. Phosphatidylinositol 4,5-Diphosphate 118-122 phospholipase C delta 1 Homo sapiens 33-42 8387776-7 1993 These showed that 50% binding of PLC delta occurred at a level of 0.9 nmol/ml PIP2 with 80 nmol/ml PC; at 2.2 nmol/ml PIP2 with 170 nmol/ml PS; at 4.2 nmol/ml PIP2 with 320 nmol/ml PI; and at 0.26 nmol/ml PIP2 with 20 nmol/ml total liver phospholipids. Phosphatidylinositol 4,5-Diphosphate 118-122 phospholipase C delta 1 Homo sapiens 33-42 8387776-12 1993 Under physiological conditions a considerable fraction of PLC delta may be bound to cellular membranes, either in an inactive form if bound to PIP2 at low resting Ca2+ concentrations, or in the inhibited form if bound to SM. Phosphatidylinositol 4,5-Diphosphate 143-147 phospholipase C delta 1 Homo sapiens 58-67 34048227-4 2021 By applying inositol triphosphate (IP3) to samples during the unroofing process, we measured a much larger koff of 1.54 +- 0.42 s-1 for PLCdelta1-PH-GFP, indicating that rebinding events are significantly suppressed through competitive action by IP3 for the same PH domain binding site as phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 289-326 phospholipase C delta 1 Homo sapiens 136-145 34048227-4 2021 By applying inositol triphosphate (IP3) to samples during the unroofing process, we measured a much larger koff of 1.54 +- 0.42 s-1 for PLCdelta1-PH-GFP, indicating that rebinding events are significantly suppressed through competitive action by IP3 for the same PH domain binding site as phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidylinositol 4,5-Diphosphate 328-332 phospholipase C delta 1 Homo sapiens 136-145 34048227-5 2021 We discuss the complex character of our PLCdelta1-PH-GFP fluorescence decays in the context of membrane receptor and ligand theory to address the question of how free PIP2 levels modulate the interaction between membrane-associated proteins and the plasma membrane. Phosphatidylinositol 4,5-Diphosphate 167-171 phospholipase C delta 1 Homo sapiens 40-49