PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2466293-0 1989 Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 63-81 2472218-0 1989 EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signaling. Tyrosine 12-20 phospholipase C gamma 1 Homo sapiens 40-58 2472218-1 1989 Binding of EGF to cells expressing human EGF receptor stimulated rapid tyrosine phosphorylation of phospholipase C-II (PLC-II), as revealed by immunoblotting analysis with phosphotyrosine-specific antibodies. Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 99-117 2472218-1 1989 Binding of EGF to cells expressing human EGF receptor stimulated rapid tyrosine phosphorylation of phospholipase C-II (PLC-II), as revealed by immunoblotting analysis with phosphotyrosine-specific antibodies. Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 119-125 2472218-2 1989 Tyrosine phosphorylation of PLC-II was stimulated by low physiological concentrations of EGF (1 nM), was quantitative, and was already maximal after a 30 sec incubation with 50 nM EGF at 37 degrees C. Interestingly, antibodies specific for PLC-II were able to coimmunoprecipitate the EGF receptor and antibodies against EGF receptor also coimmunoprecipitated PLC-II. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 28-34 2472218-2 1989 Tyrosine phosphorylation of PLC-II was stimulated by low physiological concentrations of EGF (1 nM), was quantitative, and was already maximal after a 30 sec incubation with 50 nM EGF at 37 degrees C. Interestingly, antibodies specific for PLC-II were able to coimmunoprecipitate the EGF receptor and antibodies against EGF receptor also coimmunoprecipitated PLC-II. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 240-246 2472218-2 1989 Tyrosine phosphorylation of PLC-II was stimulated by low physiological concentrations of EGF (1 nM), was quantitative, and was already maximal after a 30 sec incubation with 50 nM EGF at 37 degrees C. Interestingly, antibodies specific for PLC-II were able to coimmunoprecipitate the EGF receptor and antibodies against EGF receptor also coimmunoprecipitated PLC-II. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 240-246 2472218-4 1989 The protein tyrosine kinase inhibitor tyrphostin RG50864, which blocks EGF-dependent cell proliferation, blocked EGF-induced tyrosine phosphorylation of PLC-II, its association with EGF receptor, and EGF-induced Ca2+ release. Tyrosine 12-20 phospholipase C gamma 1 Homo sapiens 153-159 2472218-5 1989 Hence, EGF-induced tyrosine phosphorylation of PLC-II may be a regulatory event linking the tyrosine kinase activity of EGF receptor to the PIP2 hydrolysis signaling pathway. Tyrosine 19-27 phospholipase C gamma 1 Homo sapiens 47-53 2466293-7 1989 Finally, using monoclonal antibodies that specifically recognize three distinct PLC isozymes, we show that an approximately 145-kDa PLC isozyme (PLC-II) is present in A-431 cells and that EGF treatment of A-431 cells stimulates phosphorylation of PLC-II on both tyrosine and serine residues. Tyrosine 262-270 phospholipase C gamma 1 Homo sapiens 145-151 32304729-9 2020 Activated Src phosphorylated the tyrosine residue(s) on Syk molecules, which in turn interacted with phospholipase C gamma1 to trigger the translocation of PKCbetaII to the cell membrane by elevating cellular diacylglycerol levels. Tyrosine 33-41 phospholipase C gamma 1 Homo sapiens 101-123 31889510-1 2019 Direct activation of the human phospholipase C-g isozymes (PLC-g1, -g2) by tyrosine phosphorylation is fundamental to the control of diverse biological processes, including chemotaxis, platelet aggregation, and adaptive immunity. Tyrosine 75-83 phospholipase C gamma 1 Homo sapiens 59-70 25916191-2 2015 In T cells, the Tec family kinase, interleukin-2-induced tyrosine kinase (ITK), phosphorylates PLCgamma1 at tyrosine 783 (Y783) leading to activation of phospholipase function and subsequent production of the second messengers inositol 1,4,5-trisphosphate and diacylglycerol. Tyrosine 57-65 phospholipase C gamma 1 Homo sapiens 95-104 30165102-6 2018 Western blot studies showed that both ErbB receptor and PLC-gamma1 tyrosine phosphorylation levels were diminished in EGF and beta-Heregulin co-treated MDA-NEO and MDA-HER2 cells, which was further correlated to a significantly impaired calcium influx. Tyrosine 67-75 phospholipase C gamma 1 Homo sapiens 56-66 29524543-4 2018 Loss of endogenous PGP expression amplified both EGF-induced EGF receptor autophosphorylation and Src-dependent tyrosine phosphorylation of phospholipase C-gamma1 (PLCgamma1). Tyrosine 112-120 phospholipase C gamma 1 Homo sapiens 140-162 28644030-6 2017 These data revealed a previously unappreciated role for PLC-gamma1 in the positive regulation of Zap-70 and T-cell receptor tyrosine phosphorylation. Tyrosine 124-132 phospholipase C gamma 1 Homo sapiens 56-66 25916191-5 2015 The SLP-76 pY(173) motif competes with the autoinhibited conformation surrounding the SH2C domain of PLCgamma1 leading to exposure of the ITK recognition element on the PLCgamma1 SH2 domain and release of the target tyrosine, Y783. Tyrosine 216-224 phospholipase C gamma 1 Homo sapiens 101-110 23613900-8 2013 PKG II inhibited EGF-induced migration activity and blocked EGF-initiated signal transduction of PLCgamma1 and MAPK/ERK-mediated pathways through preventing EGF-induced Tyr 992 and Tyr 1068 phosphorylation of EGFR. Tyrosine 169-172 phospholipase C gamma 1 Homo sapiens 97-106 23880762-6 2013 We report that overexpression of Mn-SOD enhances tyrosine phosphorylation of TCR-associated membrane proximal signal transduction molecules Lck, LAT, ZAP70, PLCgamma1, and SLP76 within 1 min of TCR cross-linking. Tyrosine 49-57 phospholipase C gamma 1 Homo sapiens 157-166 25734483-6 2015 Once phosphorylated at tyrosine 783, PLCgamma1 enables a Ca2+-mediated, caspase-independent programmed cell death (PCD) pathway that is not down-modulated by the lymphocyte microenvironment. Tyrosine 23-31 phospholipase C gamma 1 Homo sapiens 37-46 25316710-3 2015 Previous studies showed that mutation of three tyrosine residues, Tyr(112), Tyr(128), and Tyr(145), in the N terminus of SLP-76 results in severely impaired phosphorylation and activation of Itk and PLCgamma1, which leads to defective calcium mobilization, Erk activation, and NFAT activation. Tyrosine 47-55 phospholipase C gamma 1 Homo sapiens 199-208 25316710-3 2015 Previous studies showed that mutation of three tyrosine residues, Tyr(112), Tyr(128), and Tyr(145), in the N terminus of SLP-76 results in severely impaired phosphorylation and activation of Itk and PLCgamma1, which leads to defective calcium mobilization, Erk activation, and NFAT activation. Tyrosine 66-69 phospholipase C gamma 1 Homo sapiens 199-208 25316710-7 2015 In addition, N-terminal tyrosine sites of SLP-76 also perturbed phosphorylation of Tyr(440) of Fyn, Tyr(702) of PLCgamma1, Tyr(204), Tyr(397), and Tyr(69) of ZAP-70, revealing new modes of regulation on these sites. Tyrosine 24-32 phospholipase C gamma 1 Homo sapiens 112-121 24412752-3 2014 The current model is that phosphorylation of LAT tyrosine 132 facilitates the recruitment of PLC-gamma1, leading to its activation and function at the LAT complex. Tyrosine 49-57 phospholipase C gamma 1 Homo sapiens 93-103 24412752-5 2014 We observed that commencement of the phosphorylation of LAT tyrosine 132 and PLC-gamma1 tyrosine 783 occurred simultaneously, supporting the current model. Tyrosine 88-96 phospholipase C gamma 1 Homo sapiens 77-87 23613900-8 2013 PKG II inhibited EGF-induced migration activity and blocked EGF-initiated signal transduction of PLCgamma1 and MAPK/ERK-mediated pathways through preventing EGF-induced Tyr 992 and Tyr 1068 phosphorylation of EGFR. Tyrosine 181-184 phospholipase C gamma 1 Homo sapiens 97-106 22454520-4 2012 Here we demonstrate that PDK1 regulates PLCgamma1 activation in a mechanism involving association of the two enzymes and modulation of PLCgamma1 tyrosine phosphorylation. Tyrosine 145-153 phospholipase C gamma 1 Homo sapiens 40-49 23219468-2 2013 Itk catalyzes phosphorylation on tyrosine residues within a number of its natural substrates, including the well-characterized Y783 of PLCgamma1. Tyrosine 33-41 phospholipase C gamma 1 Homo sapiens 135-144 22454520-4 2012 Here we demonstrate that PDK1 regulates PLCgamma1 activation in a mechanism involving association of the two enzymes and modulation of PLCgamma1 tyrosine phosphorylation. Tyrosine 145-153 phospholipase C gamma 1 Homo sapiens 135-144 21760611-4 2011 We show that CD95 promotes Tyr 783 phosphorylation of phospholipase C-gamma1 through the platelet-derived growth factor receptor-beta, resulting in ligand-stimulated phosphatidylinositol (4,5)-bisphosphate (PIP(2)) hydrolysis. Tyrosine 27-30 phospholipase C gamma 1 Homo sapiens 54-76 21463338-8 2011 Ethanol decreases tyrosine phosphorylation and activation of upstream signaling proteins PLCgamma1, LAT, ZAP70, and Lck. Tyrosine 18-26 phospholipase C gamma 1 Homo sapiens 89-98 19166869-4 2009 In the present study we demonstrated that BPQs not only induced EGFR tyrosine autophosphorylation, but also induced EGFR-dependent tyrosine phosphorylation of phospholipase C-gamma1 and several signal transducers and activators of transcription (STATs). Tyrosine 131-139 phospholipase C gamma 1 Homo sapiens 159-181 21471003-0 2011 Tyrosine phosphorylation-dependent activation of TRPC6 regulated by PLC-gamma1 and nephrin: effect of mutations associated with focal segmental glomerulosclerosis. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 68-78 21471003-4 2011 We demonstrate here that tyrosine phosphorylation of TRPC6 induces a complex formation with phospholipase C (PLC)-gamma1, which is prerequisite for TRPC6 surface expression. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 92-120 21123182-6 2011 Ultimately a variety of in vitro and in vivo approaches were used to verify the prediction that the tyrosine phosphorylation levels of five high-ranking substrates, PLC-gamma1, Gab1, SHP2, EGFR, and SHP1, are indeed specifically modulated by PTP1B. Tyrosine 100-108 phospholipase C gamma 1 Homo sapiens 165-175 19427038-2 2009 TCR activation results in the tyrosine phosphorylation of LAT, leading to the direct interaction with several proteins, including PLC-gamma 1, Grb2 and Gads. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 130-141 19179337-7 2009 Upon this clustering, PLC-gamma1 was bound to phosphorylated Nephrin Tyr-1204, which induced translocation of PLC-gamma1 from cytoplasm to the CD8/Nephrin cluster on the plasma membrane. Tyrosine 69-72 phospholipase C gamma 1 Homo sapiens 22-32 19179337-7 2009 Upon this clustering, PLC-gamma1 was bound to phosphorylated Nephrin Tyr-1204, which induced translocation of PLC-gamma1 from cytoplasm to the CD8/Nephrin cluster on the plasma membrane. Tyrosine 69-72 phospholipase C gamma 1 Homo sapiens 110-120 19179337-8 2009 The recruitment of PLC-gamma1 to Nephrin activated PLC-gamma1, as detected by phosphorylation of PLC-gamma1 Tyr-783 and increase in inositol 1,4,5-trisphosphate level. Tyrosine 108-111 phospholipase C gamma 1 Homo sapiens 19-29 19179337-8 2009 The recruitment of PLC-gamma1 to Nephrin activated PLC-gamma1, as detected by phosphorylation of PLC-gamma1 Tyr-783 and increase in inositol 1,4,5-trisphosphate level. Tyrosine 108-111 phospholipase C gamma 1 Homo sapiens 51-61 19179337-8 2009 The recruitment of PLC-gamma1 to Nephrin activated PLC-gamma1, as detected by phosphorylation of PLC-gamma1 Tyr-783 and increase in inositol 1,4,5-trisphosphate level. Tyrosine 108-111 phospholipase C gamma 1 Homo sapiens 51-61 19179337-9 2009 We also found that Nephrin Tyr-1204 phosphorylation triggers the Ca(2+) response in a PLC-gamma1-dependent fashion. Tyrosine 27-30 phospholipase C gamma 1 Homo sapiens 86-96 19716804-4 2009 PLC-gamma-1 was used as a substrate immobilized on a ProteoChip and incubated with an EGFR kinase to phosphorylate tyrosine residues of the substrate, followed by a fluorescence detection of the substrate recognized by a phospho-specific monoclonal antibody. Tyrosine 115-123 phospholipase C gamma 1 Homo sapiens 0-11 19166869-7 2009 PLC-gamma1 phosphorylation correlated with the phosphorylation of tyrosine-Y992, a proposed docking site for PLC-gamma1 on the EGFR. Tyrosine 66-74 phospholipase C gamma 1 Homo sapiens 0-10 19166869-7 2009 PLC-gamma1 phosphorylation correlated with the phosphorylation of tyrosine-Y992, a proposed docking site for PLC-gamma1 on the EGFR. Tyrosine 66-74 phospholipase C gamma 1 Homo sapiens 109-119 18004076-8 2008 In acute studies, H2O2 rapidly caused tyrosine phosphorylation of PLCgamma1. Tyrosine 38-46 phospholipase C gamma 1 Homo sapiens 66-75 17439160-1 2007 During T cell signaling, Itk selectively phosphorylates a tyrosine within its own SH3 domain and a tyrosine within PLCgamma1. Tyrosine 99-107 phospholipase C gamma 1 Homo sapiens 115-124 17561374-1 2007 Phospholipase Cgamma1 (PLCgamma1) represents a major downstream signalling component of the epidermal growth factor (EGF) receptor (EGFR) and is activated by tyrosine phosphorylation. Tyrosine 158-166 phospholipase C gamma 1 Homo sapiens 0-21 17561374-1 2007 Phospholipase Cgamma1 (PLCgamma1) represents a major downstream signalling component of the epidermal growth factor (EGF) receptor (EGFR) and is activated by tyrosine phosphorylation. Tyrosine 158-166 phospholipase C gamma 1 Homo sapiens 23-32 17561374-2 2007 Here we show for the first time that cellular knockdown of protein kinase Cepsilon (PKCepsilon) leads to decreased activation of PLCgamma1 by EGF and that EGF induces tyrosine phosphorylation of PKCepsilon as well as association of PKCepsilon with both EGFR and PLCgamma1. Tyrosine 167-175 phospholipase C gamma 1 Homo sapiens 262-271 17561374-4 2007 Furthermore, we identified a single tyrosine residue, PKCepsilon-Y573, within a consensus binding sequence of the C-terminal SH2 domain of PLCgamma1 which is critical for both tyrosine phosphorylation of PKCepsilon and its association with PLCgamma1. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 139-148 17561374-4 2007 Furthermore, we identified a single tyrosine residue, PKCepsilon-Y573, within a consensus binding sequence of the C-terminal SH2 domain of PLCgamma1 which is critical for both tyrosine phosphorylation of PKCepsilon and its association with PLCgamma1. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 240-249 17561374-4 2007 Furthermore, we identified a single tyrosine residue, PKCepsilon-Y573, within a consensus binding sequence of the C-terminal SH2 domain of PLCgamma1 which is critical for both tyrosine phosphorylation of PKCepsilon and its association with PLCgamma1. Tyrosine 176-184 phospholipase C gamma 1 Homo sapiens 139-148 17561374-4 2007 Furthermore, we identified a single tyrosine residue, PKCepsilon-Y573, within a consensus binding sequence of the C-terminal SH2 domain of PLCgamma1 which is critical for both tyrosine phosphorylation of PKCepsilon and its association with PLCgamma1. Tyrosine 176-184 phospholipase C gamma 1 Homo sapiens 240-249 17561374-6 2007 Thereby the tyrosine phosphorylation of PLCgamma1 via the EGFR may be facilitated. Tyrosine 12-20 phospholipase C gamma 1 Homo sapiens 40-49 17652306-4 2007 ITK is thought to phosphorylate a specific tyrosine residue of PLC-gamma1 that is required for its activation. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 63-73 17494698-7 2007 This interaction occurs through an Src homology 2 domain of PLCgamma1 and requires the EphA4 juxtamembrane tyrosines. Tyrosine 107-116 phospholipase C gamma 1 Homo sapiens 60-69 18004076-3 2008 Stimulation of PLCgamma1 was assessed by immunoblots of tyrosine phosphorylation. Tyrosine 56-64 phospholipase C gamma 1 Homo sapiens 15-24 17116690-3 2007 Mutation of the SH2C domain tyrosine binding site led to constitutive PLC-gamma1 activation. Tyrosine 28-36 phospholipase C gamma 1 Homo sapiens 70-80 17372230-5 2007 The tertiary complex formation between VEGFR-2, PLCgamma1 and c-Cbl selectively promotes ubiquitylation and suppression of tyrosine phosphorylation of PLCgamma1 by a proteolysis-independent mechanism. Tyrosine 123-131 phospholipase C gamma 1 Homo sapiens 48-57 17372230-5 2007 The tertiary complex formation between VEGFR-2, PLCgamma1 and c-Cbl selectively promotes ubiquitylation and suppression of tyrosine phosphorylation of PLCgamma1 by a proteolysis-independent mechanism. Tyrosine 123-131 phospholipase C gamma 1 Homo sapiens 151-160 17220479-5 2007 Interestingly, in these conditions PLCgamma1 phosphorylation in the regulatory tyrosine 783 is also defective. Tyrosine 79-87 phospholipase C gamma 1 Homo sapiens 35-44 17116690-5 2007 PLC-gamma1 constructs with mutations in tyrosine 509 and phenylalanine 510 in the sPHN domain no longer required an intact amino-terminal Src homology (SH2N) domain or phosphorylation of tyrosine 775 or 783 for activation. Tyrosine 40-48 phospholipase C gamma 1 Homo sapiens 0-10 17116690-5 2007 PLC-gamma1 constructs with mutations in tyrosine 509 and phenylalanine 510 in the sPHN domain no longer required an intact amino-terminal Src homology (SH2N) domain or phosphorylation of tyrosine 775 or 783 for activation. Tyrosine 187-195 phospholipase C gamma 1 Homo sapiens 0-10 16038803-0 2005 Grb2 negatively regulates epidermal growth factor-induced phospholipase C-gamma1 activity through the direct interaction with tyrosine-phosphorylated phospholipase C-gamma1. Tyrosine 126-134 phospholipase C gamma 1 Homo sapiens 58-80 17050525-3 2006 Here, we report that the sequences surrounding the Vav1 AC: Tyr(142), Tyr(160), and Tyr(174) are evolutionarily conserved, conform to consensus SH2 domain binding motifs, and bind several proteins implicated in TCR signaling, including Lck, PI3K p85alpha, and PLCgamma1, through direct interactions with their SH2 domains. Tyrosine 60-63 phospholipase C gamma 1 Homo sapiens 260-269 17050525-3 2006 Here, we report that the sequences surrounding the Vav1 AC: Tyr(142), Tyr(160), and Tyr(174) are evolutionarily conserved, conform to consensus SH2 domain binding motifs, and bind several proteins implicated in TCR signaling, including Lck, PI3K p85alpha, and PLCgamma1, through direct interactions with their SH2 domains. Tyrosine 70-73 phospholipase C gamma 1 Homo sapiens 260-269 17050525-3 2006 Here, we report that the sequences surrounding the Vav1 AC: Tyr(142), Tyr(160), and Tyr(174) are evolutionarily conserved, conform to consensus SH2 domain binding motifs, and bind several proteins implicated in TCR signaling, including Lck, PI3K p85alpha, and PLCgamma1, through direct interactions with their SH2 domains. Tyrosine 70-73 phospholipase C gamma 1 Homo sapiens 260-269 16636972-2 2006 Resveratrol inhibited mast cell degranulation in a dose-dependent manner and reduced the FcepsilonRI-mediated tyrosine phosphorylation of ERK and PLCgamma1 but not of Syk and PLCgamma2. Tyrosine 110-118 phospholipase C gamma 1 Homo sapiens 146-155 16636972-4 2006 These results suggest that FcepsilonRI-mediated tyrosine phosphorylation of PLCgamma1 and ERK could be potential cellular targets of resveratrol for the inhibition of mast cell degranulation. Tyrosine 48-56 phospholipase C gamma 1 Homo sapiens 76-85 15936927-5 2006 In cardiomyocytes, only PDGF stimulated tyrosine phosphorylation of PLCgamma1 and nPKCdelta. Tyrosine 40-48 phospholipase C gamma 1 Homo sapiens 68-77 16467851-1 2006 Engagement of the T-cell antigen receptor leads to recruitment of phospholipase Cgamma1 (PLCgamma1) to the LAT-nucleated signaling complex and to PLCgamma1 activation in a tyrosine phosphorylation-dependent manner. Tyrosine 172-180 phospholipase C gamma 1 Homo sapiens 66-87 16467851-1 2006 Engagement of the T-cell antigen receptor leads to recruitment of phospholipase Cgamma1 (PLCgamma1) to the LAT-nucleated signaling complex and to PLCgamma1 activation in a tyrosine phosphorylation-dependent manner. Tyrosine 172-180 phospholipase C gamma 1 Homo sapiens 89-98 16467851-1 2006 Engagement of the T-cell antigen receptor leads to recruitment of phospholipase Cgamma1 (PLCgamma1) to the LAT-nucleated signaling complex and to PLCgamma1 activation in a tyrosine phosphorylation-dependent manner. Tyrosine 172-180 phospholipase C gamma 1 Homo sapiens 146-155 16291968-4 2005 Moreover, the cAMP-dependent tyrosine phosphorylation was also induced at the key regulatory residue of PLCgamma1 in the same segments of spermatozoa, but it was inhibited by the addition of herbimycin A (a tyrosine kinase inhibitor; 5 microM). Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 104-113 16038803-0 2005 Grb2 negatively regulates epidermal growth factor-induced phospholipase C-gamma1 activity through the direct interaction with tyrosine-phosphorylated phospholipase C-gamma1. Tyrosine 126-134 phospholipase C gamma 1 Homo sapiens 150-172 16038803-3 2005 In this study, we demonstrate for the first time that Grb2, an adaptor protein, specifically interacts with tyrosine-phosphorylated PLC-gamma1 at Tyr783. Tyrosine 108-116 phospholipase C gamma 1 Homo sapiens 132-142 16038803-5 2005 Replacement of Tyr783 with Phe completely blocked EGF-induced interaction of PLC-gamma1 with Grb2, indicating that tyrosine phosphorylation of PLC-gamma1 at Tyr783 is essential for the interaction with Grb2. Tyrosine 115-123 phospholipase C gamma 1 Homo sapiens 77-87 16038803-5 2005 Replacement of Tyr783 with Phe completely blocked EGF-induced interaction of PLC-gamma1 with Grb2, indicating that tyrosine phosphorylation of PLC-gamma1 at Tyr783 is essential for the interaction with Grb2. Tyrosine 115-123 phospholipase C gamma 1 Homo sapiens 143-153 15764700-0 2005 Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 114-136 16081816-6 2005 In additions, we provide evidence that ZAP-70 is the primary in vivo kinase for LAT tyrosine 191 and that Itk plays a role in the phosphorylation of tyrosine 783 on phospholipase C-gamma1. Tyrosine 149-157 phospholipase C gamma 1 Homo sapiens 165-187 15673613-5 2005 A tyrosine mutant VEGFR-2, defective in PLC-gamma1 activation underwent down-regulation efficiently in response to ligand stimulation, suggesting that activation of classical PKCs are not involved in VEGFR-2 down-regulation. Tyrosine 15-23 phospholipase C gamma 1 Homo sapiens 53-63 15623534-2 2005 T cell receptor (TCR)-induced activation of phospholipase C-gamma1 (PLC-gamma1) depends on three features of SLP-76: the N-terminal tyrosine phosphorylation sites, the Gads-binding site, and an intervening sequence, denoted the P-I region, which binds to the SH3 domain of PLC-gamma1 (SH3(PLC)) via a low affinity interaction. Tyrosine 132-140 phospholipase C gamma 1 Homo sapiens 44-66 15623534-2 2005 T cell receptor (TCR)-induced activation of phospholipase C-gamma1 (PLC-gamma1) depends on three features of SLP-76: the N-terminal tyrosine phosphorylation sites, the Gads-binding site, and an intervening sequence, denoted the P-I region, which binds to the SH3 domain of PLC-gamma1 (SH3(PLC)) via a low affinity interaction. Tyrosine 132-140 phospholipase C gamma 1 Homo sapiens 68-78 15657076-8 2005 Adhesion to fibronectin induced PLC-gamma1 tyrosine phosphorylation that was inhibited by a Src-kinase inhibitor, but not an epidermal-growth-factor-receptor kinase inhibitor. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 32-42 15657076-9 2005 Moreover, in cells null for Src family members, but not in cells null for FAK family members, integrin-dependent PLC-gamma1 tyrosine phosphorylation was greatly reduced. Tyrosine 124-132 phospholipase C gamma 1 Homo sapiens 113-123 15641795-1 2005 The signal transduction protein phospholipase C-gamma1 (PLC-gamma1) is activated when its C-terminal SH2 domain (PLCC) binds the phosphorylated Tyr-1021 site (pTyr-1021) in the beta-platelet-derived growth factor receptor (PDGFR). Tyrosine 144-147 phospholipase C gamma 1 Homo sapiens 56-66 12771140-7 2003 Compared with untreated cells, tyrosine phosphorylation of phospholipase C-gamma1 was enhanced by EGF stimulation in glucosylceramide-depleted cells, associated with enhanced tyrosine phosphorylation of the EGF receptor at Tyr-1068 and Tyr-1086 stimulated by EGF. Tyrosine 31-39 phospholipase C gamma 1 Homo sapiens 59-81 16706231-5 2005 In contrast, tyrphostin AG1478 abrogates tyrosine phosphorylation of PLCgamma1 and STAT3. Tyrosine 41-49 phospholipase C gamma 1 Homo sapiens 69-78 14568990-4 2003 Insulin increased PLCgamma1 tyrosine phosphorylation at Tyr-783 and its colocalization with the IR in punctated structures enriched in cortical actin at the dorsal plasma membrane. Tyrosine 28-36 phospholipase C gamma 1 Homo sapiens 18-27 14568990-4 2003 Insulin increased PLCgamma1 tyrosine phosphorylation at Tyr-783 and its colocalization with the IR in punctated structures enriched in cortical actin at the dorsal plasma membrane. Tyrosine 56-59 phospholipase C gamma 1 Homo sapiens 18-27 12890758-5 2003 Staurosporine treatment induced relocation of tyrosine phosphorylated phospholipase C-gamma1 (PLC-gamma1) to the tips of lamellipodia where actin assembly was initiated. Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 70-92 12890758-5 2003 Staurosporine treatment induced relocation of tyrosine phosphorylated phospholipase C-gamma1 (PLC-gamma1) to the tips of lamellipodia where actin assembly was initiated. Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 94-104 12941616-2 2003 Analysis of site-specific c-Cbl mutants indicated that tyrosine phosphorylation of c-Cbl was required for down-regulation of the PLCgamma1/Ca2+ pathway. Tyrosine 55-63 phospholipase C gamma 1 Homo sapiens 129-138 15214048-2 2004 Here, we report that the TCR/CD28-induced tyrosine phosphorylation and activation of PLCgamma1 was significantly impaired in PKCtheta (-/-) primary, restimulated T cells. Tyrosine 42-50 phospholipase C gamma 1 Homo sapiens 85-94 14710234-4 2004 PS2-TAT treatment of the EGFR/c-erbB-2-positive cell line MDA-HER2 resulted in a reduction of the EGF-mediated PLC-gamma1 tyrosine phosphorylation of about 30%, concomitant with a complete abrogation of the EGF-driven calcium influx. Tyrosine 122-130 phospholipase C gamma 1 Homo sapiens 111-121 12771140-7 2003 Compared with untreated cells, tyrosine phosphorylation of phospholipase C-gamma1 was enhanced by EGF stimulation in glucosylceramide-depleted cells, associated with enhanced tyrosine phosphorylation of the EGF receptor at Tyr-1068 and Tyr-1086 stimulated by EGF. Tyrosine 175-183 phospholipase C gamma 1 Homo sapiens 59-81 12771140-7 2003 Compared with untreated cells, tyrosine phosphorylation of phospholipase C-gamma1 was enhanced by EGF stimulation in glucosylceramide-depleted cells, associated with enhanced tyrosine phosphorylation of the EGF receptor at Tyr-1068 and Tyr-1086 stimulated by EGF. Tyrosine 223-226 phospholipase C gamma 1 Homo sapiens 59-81 12771140-7 2003 Compared with untreated cells, tyrosine phosphorylation of phospholipase C-gamma1 was enhanced by EGF stimulation in glucosylceramide-depleted cells, associated with enhanced tyrosine phosphorylation of the EGF receptor at Tyr-1068 and Tyr-1086 stimulated by EGF. Tyrosine 236-239 phospholipase C gamma 1 Homo sapiens 59-81 12771140-8 2003 The Src inhibitor, PP2, significantly blocked EGF-induced tyrosine phosphorylation of phospholipase C-gamma1 in control cells, whereas in glucosylceramide-depleted cells, suppression of Src kinase activity by PP2 toward EGF-induced tyrosine phosphorylation of phospholipase C-gamma1 was less significant. Tyrosine 58-66 phospholipase C gamma 1 Homo sapiens 86-108 12771140-8 2003 The Src inhibitor, PP2, significantly blocked EGF-induced tyrosine phosphorylation of phospholipase C-gamma1 in control cells, whereas in glucosylceramide-depleted cells, suppression of Src kinase activity by PP2 toward EGF-induced tyrosine phosphorylation of phospholipase C-gamma1 was less significant. Tyrosine 232-240 phospholipase C gamma 1 Homo sapiens 86-108 12717426-3 2003 70Z/3 Cbl-induced PLC gamma 1 tyrosine phosphorylation required, in addition to the PLC gamma 1 N-terminal SH2 domain, the C-terminal SH2 and SH3 domains that were dispensable for TCR-induced phosphorylation. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 18-29 12866655-6 2003 A tyrosine phosphorylation of PLC-gamma1 was observed in concomitance with the ATRA-induced maximal functional activity. Tyrosine 2-10 phospholipase C gamma 1 Homo sapiens 30-40 12598525-6 2003 Further analysis showed that tyrosine 1006 is responsible for phospholipase Cgamma1 (PLCgamma1) activation and intracellular calcium release in endothelial cells. Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 85-94 12598525-7 2003 Activation of PLCgamma1 was selectively mediated by tyrosine 1006. Tyrosine 52-60 phospholipase C gamma 1 Homo sapiens 14-23 12598525-9 2003 Association of VEGFR-2 with PLCgamma1 was mainly established between tyrosine 1006 and the C-terminal SH2 domain of PLCgamma1 in vitro and in vivo. Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 28-37 12598525-10 2003 Taken together, the results indicate that phosphorylation of tyrosine 1006 is essential for VEGFR-2-mediated PLCgamma1 activation, calcium flux, and cell differentiation. Tyrosine 61-69 phospholipase C gamma 1 Homo sapiens 109-118 12496416-5 2003 Grb2, Gads, and PLC-gamma1 associated with LAT preferentially via different sets of tyrosine residues; however, they failed to interact with LAT mutants containing only one tyrosine. Tyrosine 84-92 phospholipase C gamma 1 Homo sapiens 16-26 12373311-7 2002 This observation could be explained by the fact that the PLCgamma1 association sites in the EGFR, tyrosine residues 992 and 1173, were phosphorylated to a lower degree when the receptor was stimulated with EGF-dextran as compared to with EGF. Tyrosine 98-106 phospholipase C gamma 1 Homo sapiens 57-66 12354693-3 2002 EGF stimulation of EGF receptor (EGFR) overexpressing cells resulted in long-term PLC-gamma1 tyrosine phosphorylation and sustained levels of inositol-1,4,5-triphosphate (IP3) and diacylglycerol (DAG) producing sinusoidal calcium oscillations. Tyrosine 93-101 phospholipase C gamma 1 Homo sapiens 82-92 12354693-4 2002 In contrast, c-erbB-2/EGFR expressing cells displayed baseline transient calcium oscillations after EGF treatment due to short-term PLC-gamma1 tyrosine phosphorylation and short-term IP3 and DAG turnover. Tyrosine 143-151 phospholipase C gamma 1 Homo sapiens 132-142 11606584-2 2001 The importance of growth factor-stimulated phosphorylation of specific tyrosine residues has been documented for PLCgamma1; however, despite the critical importance of PLCgamma2 in B-cell signal transduction, neither the tyrosine kinase(s) that directly phosphorylate PLCgamma2 nor the sites in PLCgamma2 that become phosphorylated after stimulation are known. Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 113-122 11823862-2 2002 PLC-gamma 1 also has mitogenic activity upon growth-factor-dependent tyrosine phosphorylation; however, this activity is not dependent on the phospholipase activity of PLC-gamma 1, but requires an SH3 domain. Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 0-11 12372399-0 2002 Prostaglandin F(2alpha) stimulates tyrosine phosphorylation of phospholipase C-gamma1. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 63-85 12372399-1 2002 In this study, we investigated the ability of prostaglandin F(2alpha) (PGF(2alpha)) to induce tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) in cat iris sphincter smooth muscle (CISM) cells. Tyrosine 94-102 phospholipase C gamma 1 Homo sapiens 122-144 12372399-1 2002 In this study, we investigated the ability of prostaglandin F(2alpha) (PGF(2alpha)) to induce tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) in cat iris sphincter smooth muscle (CISM) cells. Tyrosine 94-102 phospholipase C gamma 1 Homo sapiens 146-156 12372399-2 2002 PGF(2alpha)(1 microM) stimulated PLC-gamma1 tyrosine phosphorylation in a time- and dose-dependent manner with a maximum increase of 3-fold at 0.5min. Tyrosine 44-52 phospholipase C gamma 1 Homo sapiens 33-43 12372399-5 2002 In summary, these findings show that PGF(2alpha) stimulates tyrosine phosphorylation of PLC-gamma1 in CISM cells and indicate that PGF(2alpha)-stimulated tyrosine phosphorylation is responsible for an early signal transduction event. Tyrosine 60-68 phospholipase C gamma 1 Homo sapiens 88-98 12372399-5 2002 In summary, these findings show that PGF(2alpha) stimulates tyrosine phosphorylation of PLC-gamma1 in CISM cells and indicate that PGF(2alpha)-stimulated tyrosine phosphorylation is responsible for an early signal transduction event. Tyrosine 154-162 phospholipase C gamma 1 Homo sapiens 88-98 12163161-7 2002 Furthermore, this deletion reduces the ability of the Src family kinase Lck to activate ITK, as well as to induce the ITK mediated tyrosine phosphorylation of its substrate PLCgamma1. Tyrosine 131-139 phospholipase C gamma 1 Homo sapiens 173-182 11750651-6 2002 CD28 crosslinking on YT-Indy-cl43 enhanced tyrosine phosphorylation of PLC-gamma1. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 71-81 11750651-7 2002 The simultaneous ligation of KIR2DL2 with mAb resulted in a decrease in CD28-induced tyrosine phosphorylation of PLC-gamma1 confirming that dephosphorylation of this protein is involved in the KIR2DL2-induced inhibition of CD28-mediated cytotoxicity. Tyrosine 85-93 phospholipase C gamma 1 Homo sapiens 113-123 11457888-3 2001 In the Jurkat T cell line, the distal four tyrosines of LAT bind PLCgamma-1, Grb2, and Gads. Tyrosine 43-52 phospholipase C gamma 1 Homo sapiens 65-75 11395491-6 2001 These tyrosine residues function by reconstituting PLC-gamma(1) phosphorylation and recruitment to LAT. Tyrosine 6-14 phospholipase C gamma 1 Homo sapiens 51-63 11753673-6 2001 Tyrosine phosphorylation stimulates PI3K and PLCgamma-1 enzymatic activity, and on ShcA creates binding sites for Grb2 with its associated Sos1 and Gab1. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 45-55 11585897-8 2001 CD3 stimulation of P116 cells also induced tyrosine phosphorylation of phospholipase C-gamma1 (PLCgamma1) and increased the intracellular Ca(2+) concentration. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 71-93 11585897-8 2001 CD3 stimulation of P116 cells also induced tyrosine phosphorylation of phospholipase C-gamma1 (PLCgamma1) and increased the intracellular Ca(2+) concentration. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 95-104 11585897-10 2001 The physiologic relevance of these signaling events is further supported by the finding of PLCgamma1 tyrosine phosphorylation, Erk activation, and CD69 upregulation in P116 cells on stimulation with superantigen and antigen-presenting cells. Tyrosine 101-109 phospholipase C gamma 1 Homo sapiens 91-100 11564877-4 2001 Raft-targeted PLCgamma1 was constitutively tyrosine phosphorylated and induced constitutive NF-AT-dependent transcription and interleukin-2 secretion in Jurkat cells. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 14-23 11564877-5 2001 Tyrosine phosphorylation of raft-targeted PLCgamma1 did not require Zap-70 or the interaction with the adapters Lat and Slp-76, molecules that are necessary for TCR signaling. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 42-51 11395491-2 2001 Following TCR stimulation, LAT becomes tyrosine-phosphorylated, creating docking sites for other signaling proteins such as phospholipase C-gamma(1) (PLC-gamma(1)), Grb2, and Gads. Tyrosine 39-47 phospholipase C gamma 1 Homo sapiens 124-148 11395491-2 2001 Following TCR stimulation, LAT becomes tyrosine-phosphorylated, creating docking sites for other signaling proteins such as phospholipase C-gamma(1) (PLC-gamma(1)), Grb2, and Gads. Tyrosine 39-47 phospholipase C gamma 1 Homo sapiens 150-162 11390650-2 2001 In particular, TCR-induced tyrosine phosphorylation and activation of phospholipase C-gamma1 (PLC-gamma1), and the resultant TCR-inducible gene expression, depend on SLP-76. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 94-104 10975797-5 2000 The TCR-induced tyrosine phosphorylation of phospholipase C-gamma1, SH2-domain-containing leukocyte-specific phosphoprotein of 76kDa, and linker for activation of T cells was also reduced. Tyrosine 16-24 phospholipase C gamma 1 Homo sapiens 44-66 11226408-1 2001 Upon epidermal growth factor treatment, phospholipase C-gamma1 (PLC-gamma1) translocates from cytosol to membrane where it is phosphorylated at tyrosine residues. Tyrosine 144-152 phospholipase C gamma 1 Homo sapiens 40-62 11226408-1 2001 Upon epidermal growth factor treatment, phospholipase C-gamma1 (PLC-gamma1) translocates from cytosol to membrane where it is phosphorylated at tyrosine residues. Tyrosine 144-152 phospholipase C gamma 1 Homo sapiens 64-74 11226408-3 2001 In this study, we show that the translocation of PLC-gamma1 and its tyrosine phosphorylation are localized in caveolae by caveolin-enriched low-density membrane (CM) preparation and immunostaining of cells. Tyrosine 68-76 phospholipase C gamma 1 Homo sapiens 49-59 11226410-6 2001 Cleavage of EGFR by caspase-3 significantly impaired the tyrosine phosphorylation of PLC-gamma1 in vitro. Tyrosine 57-65 phospholipase C gamma 1 Homo sapiens 85-95 11207601-3 2000 Purified InlB stimulates association of PLC-gamma1 with one or more tyrosine-phosphorylated proteins, followed by a transient increase in intracellular inositol 1,4,5-trisphosphate (IP3) levels and a release of intracellular Ca2+ in a PI 3-kinase-dependent manner. Tyrosine 68-76 phospholipase C gamma 1 Homo sapiens 40-50 11095525-6 2000 SIN-1 treatment induced tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) and induced its binding with activated TrkB, similar to that seen with BDNF downstream signaling pathways. Tyrosine 24-32 phospholipase C gamma 1 Homo sapiens 52-74 11095525-6 2000 SIN-1 treatment induced tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) and induced its binding with activated TrkB, similar to that seen with BDNF downstream signaling pathways. Tyrosine 24-32 phospholipase C gamma 1 Homo sapiens 76-86 11368773-5 2001 By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Tyrosine 147-155 phospholipase C gamma 1 Homo sapiens 249-270 11368773-5 2001 By substituting these tyrosine residues in LAT with phenylalanine and by utilizing phosphorylated peptides derived from these sites, we mapped the tyrosine residues in LAT required for the direct interaction and activation of Vav, p85/p110alpha and phospholipase Cgamma1 (PLCgamma1). Tyrosine 147-155 phospholipase C gamma 1 Homo sapiens 272-281 11093148-2 2000 Beside common biochemical events, we previously showed that a 62-kDa protein associated with PLCgamma-1 and p21RasGAP was specifically tyrosine phosphorylated after CD2 stimulation in Jurkat T cells. Tyrosine 135-143 phospholipase C gamma 1 Homo sapiens 93-103 11093148-7 2000 By contrast, CD2-induced PLCgamma-1 tyrosine phosphorylation and calcium response progressively diminished. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 25-35 11093148-8 2000 Finally, enhanced amounts of tyrosine phosphorylated p62Dok were recruited to p21RasGAP and PLCgamma-1 after CD2 stimulation in CD3-activated cells. Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 92-102 10987838-8 2000 These data show a cross-talk between LPA and EGF limited to a branch of EGFR-mediated signaling, which may be explained by a LPA-induced, G(alphai)-protein-mediated translocation of PLCgamma-1 to EGFR in the absence of detectable tyrosine phosphorylation of both proteins. Tyrosine 230-238 phospholipase C gamma 1 Homo sapiens 182-192 10760511-3 2000 The PDGF-Rbeta downstream intracellular transduction pathway including tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) and phosphatidylinositol 3"-kinase (PI 3"-K) was also inhibited. Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 99-121 10940929-6 2000 The kinetics of protein complex enhancement correlated with TCR / CD3-induced tyrosine phosphorylation of PLCgamma1; however, those PLCgamma1 molecules in complex with hSos2 were non-phosphorylated after TCR / CD3 stimulation, in contrast to the phosphorylated PLCgamma1 associated with the linker for activation of T cells, LAT. Tyrosine 78-86 phospholipase C gamma 1 Homo sapiens 106-115 10834929-8 2000 Epidermal growth factor receptor (EGFR) -induced tyrosine phosphorylation of PLC-gamma1 resulted in resistance to cleavage by caspase-3 in vitro. Tyrosine 49-57 phospholipase C gamma 1 Homo sapiens 77-87 10834929-10 2000 In addition, tyrosine-phosphorylated PLC-gamma1 was not significantly cleaved during etoposide-induced apoptosis in Molt-4 cells. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 37-47 10834929-11 2000 This suggests that the growth factor-induced tyrosine phosphorylation may suppress apoptosis-induced fragmentation of PLC-gamma1. Tyrosine 45-53 phospholipase C gamma 1 Homo sapiens 118-128 10760511-3 2000 The PDGF-Rbeta downstream intracellular transduction pathway including tyrosine phosphorylation of phospholipase C-gamma1 (PLC-gamma1) and phosphatidylinositol 3"-kinase (PI 3"-K) was also inhibited. Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 123-133 10734140-5 2000 Moreover, LTD(4) induced an increased association of c-Src with PLC-gamma1, and the selective Src family tyrosine kinase inhibitor PP1 blocked both LTD(4)-induced tyrosine phosphorylation of PLC-gamma1 and the association of PLC-gamma1 with Gbetagamma subunits. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 191-201 10734140-5 2000 Moreover, LTD(4) induced an increased association of c-Src with PLC-gamma1, and the selective Src family tyrosine kinase inhibitor PP1 blocked both LTD(4)-induced tyrosine phosphorylation of PLC-gamma1 and the association of PLC-gamma1 with Gbetagamma subunits. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 191-201 10652211-7 2000 Although direct tyrosine phosphorylation of PLCgamma1 was not detectable, the amount of PLCgamma1 coprecipitable with anti-phosphotyrosine was increased after IL-4 stimulation. Tyrosine 16-24 phospholipase C gamma 1 Homo sapiens 44-53 10692443-1 2000 Upon stimulation of cells with platelet-derived growth factor (PDGF), phospholipase C-gamma1 (PLC-gamma1) binds to the tyrosine-phosphorylated PDGF receptor through one or both of its Src homology 2 (SH2) domains, is phosphorylated by the receptor kinase, and is thereby activated to hydrolyze phosphatidylinositol 4, 5-bisphosphate. Tyrosine 119-127 phospholipase C gamma 1 Homo sapiens 70-92 10692443-1 2000 Upon stimulation of cells with platelet-derived growth factor (PDGF), phospholipase C-gamma1 (PLC-gamma1) binds to the tyrosine-phosphorylated PDGF receptor through one or both of its Src homology 2 (SH2) domains, is phosphorylated by the receptor kinase, and is thereby activated to hydrolyze phosphatidylinositol 4, 5-bisphosphate. Tyrosine 119-127 phospholipase C gamma 1 Homo sapiens 94-104 10741414-4 2000 This transiently induced tyrosine phosphorylation of multiple proteins, including the ZAP-70 tyrosine kinase, its associated T cell antigen receptor zeta chain, LAT and phospholipase Cgamma1. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 169-190 10656690-6 2000 Herein, we demonstrate that acidic substitution of the activation loop tyrosines is sufficient to induce allosteric changes required for constitutive TrkA kinase activity as well as phosphorylation of TrkA signaling proteins such as Shc, PLCgamma-1, FRS-2 and erk1/2. Tyrosine 71-80 phospholipase C gamma 1 Homo sapiens 238-248 10486198-5 1999 Using immunoprecipitation, PI3-kinase and tyrosine phosphorylated PLC-gamma1 and SHC were shown to be associated with tyrosine phosphorylated TrkB in response to both BDNF and NT-4. Tyrosine 42-50 phospholipase C gamma 1 Homo sapiens 66-76 10523627-5 1999 Tyrosine phosphorylation did not require the SH2(C) or SH3 domains but depended exclusively on a functional SH2(N) domain, which mediated the association of PLCgamma1 with the adapter protein, BLNK. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 157-166 10497192-2 1999 These events are preceded by the ligand-induced tyrosine phosphorylation of the receptor and its association with SH2-containing signaling enzymes including Src family members (Src), the phosphotyrosine phosphatase SHP-2, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-gamma1 (PLCgamma). Tyrosine 48-56 phospholipase C gamma 1 Homo sapiens 264-286 10497192-2 1999 These events are preceded by the ligand-induced tyrosine phosphorylation of the receptor and its association with SH2-containing signaling enzymes including Src family members (Src), the phosphotyrosine phosphatase SHP-2, phosphatidylinositol 3-kinase (PI3K), and phospholipase C-gamma1 (PLCgamma). Tyrosine 48-56 phospholipase C gamma 1 Homo sapiens 288-296 10486198-5 1999 Using immunoprecipitation, PI3-kinase and tyrosine phosphorylated PLC-gamma1 and SHC were shown to be associated with tyrosine phosphorylated TrkB in response to both BDNF and NT-4. Tyrosine 118-126 phospholipase C gamma 1 Homo sapiens 66-76 10381756-8 1999 Of the tyrosine-phosphorylated proteins, the results suggest that two of them are PLCgamma1 and adapter protein Shc. Tyrosine 7-15 phospholipase C gamma 1 Homo sapiens 82-91 10489101-9 1999 rHuEPO induced tyrosine phosphorylation of PLC-gamma1 and activation of PKC. Tyrosine 15-23 phospholipase C gamma 1 Homo sapiens 43-53 10350617-10 1999 This receptor was found to activate PLC-gamma1, indicating that the IR TK domain, in situ, is able to tyrosine phosphorylate substrates normally used by the EGFR. Tyrosine 102-110 phospholipase C gamma 1 Homo sapiens 36-46 10373546-4 1999 Under equilibrium incubation conditions (4 degrees C, 40 min), the N-SH2 domain, but not the C-SH2 domain, was sufficient to mediate significant PLC-gamma1 association with the activated PDGF receptor and PLC-gamma1 tyrosine phosphorylation. Tyrosine 216-224 phospholipase C gamma 1 Homo sapiens 205-215 10360968-4 1999 Using this cell line, we demonstrate that LAT is required for TCR-mediated Ca2+ mobilization and optimal tyrosine phosphorylation of phospholipase C-gamma1, Vav and SLP-76. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 133-155 10202147-6 1999 These defects were correlated with reduced tyrosine phosphorylation of phospholipase C (PLC)-gamma1 and the LAT adapter protein in the ZAP(Y319-->F)-expressing cells. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 71-99 10350061-6 1999 These results suggest that overlapping immunoreceptor tyrosine-based inhibition motif/immunoreceptor tyrosine-based activation motif-like motifs within platelet endothelial cell adhesion molecule 1 mediate differential interactions between the Src homology 2 containing signalling proteins SHP-1, SHP-2, SHIP and PLC-gamma1. Tyrosine 54-62 phospholipase C gamma 1 Homo sapiens 313-323 10100621-3 1999 The present study was aimed to elucidate the molecular target(s) of these tyrosine phosphorylations induced by HCRI and demonstrated that simvastatin induces tyrosine phosphorylation of phospholipase C (PLC) gamma1. Tyrosine 74-82 phospholipase C gamma 1 Homo sapiens 186-214 10085141-7 1999 In contrast to PIP2 hydrolysis, PLC-gamma1 tyrosine phosphorylation correlated linearly with the total level of Tyr(P)-EGFR stimulated by either ligand, indicating that the functional deficiency of internal EGFR cannot be attributed to an inability to interact with and phosphorylate signaling proteins. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 32-42 10100621-3 1999 The present study was aimed to elucidate the molecular target(s) of these tyrosine phosphorylations induced by HCRI and demonstrated that simvastatin induces tyrosine phosphorylation of phospholipase C (PLC) gamma1. Tyrosine 158-166 phospholipase C gamma 1 Homo sapiens 186-214 10100621-0 1999 Role of tyrosine phosphorylation of phospholipase C gamma1 in the signaling pathway of HMG-CoA reductase inhibitor-induced cell death of L6 myoblasts. Tyrosine 8-16 phospholipase C gamma 1 Homo sapiens 36-58 10100621-4 1999 This tyrosine phosphorylation of PLC-gamma1 caused the increment of the intracellular inositol triphosphate (IP3) levels in L6 myoblasts. Tyrosine 5-13 phospholipase C gamma 1 Homo sapiens 33-43 10100621-5 1999 Pretreatment of the cells with herbimycin A, a specific inhibitor of protein tyrosine kinase, inhibited a simvastatin-induced increase in IP3 level in the cells as well as tyrosine phosphorylation of PLC-gamma1. Tyrosine 77-85 phospholipase C gamma 1 Homo sapiens 200-210 10100621-7 1999 Thus, these results strongly suggest that simvastatin-induced tyrosine phosphorylation of PLC-gamma1 plays, at least in part, an important role for the development of simvastatin-induced cell death. Tyrosine 62-70 phospholipase C gamma 1 Homo sapiens 90-100 9822654-7 1998 Exposure of A431 cells to ONOO- markedly reduced the kinetics of tyrosine phosphorylation of a downstream EGFR substrate, phospholipase C-gamma1, which may be related to covalent alterations in EGFR. Tyrosine 65-73 phospholipase C gamma 1 Homo sapiens 122-144 9891995-0 1998 Nuclear association of tyrosine-phosphorylated Vav to phospholipase C-gamma1 and phosphoinositide 3-kinase during granulocytic differentiation of HL-60 cells. Tyrosine 23-31 phospholipase C gamma 1 Homo sapiens 54-76 9706872-8 1998 The coimmunoprecipitation of tyrosine phosphorylated PLC-gamma1 with surface MHC class II suggested that PLC-gamma1 could be recruited to MHC class II after engagement. Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 53-63 9706872-8 1998 The coimmunoprecipitation of tyrosine phosphorylated PLC-gamma1 with surface MHC class II suggested that PLC-gamma1 could be recruited to MHC class II after engagement. Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 105-115 9716455-1 1998 It is known that platelet-derived growth factor (PDGF) induces the phosphorylation of phospholipase C (PLC) gamma1 and that phosphorylation on tyrosine (Tyr) 783 of PLCgamma1 is essential for phosphatidylinositol 4,5-bisphosphate hydrolyzing activity in vivo, while phosphorylation does not affect the catalytic activity in vitro. Tyrosine 143-151 phospholipase C gamma 1 Homo sapiens 165-174 9716455-1 1998 It is known that platelet-derived growth factor (PDGF) induces the phosphorylation of phospholipase C (PLC) gamma1 and that phosphorylation on tyrosine (Tyr) 783 of PLCgamma1 is essential for phosphatidylinositol 4,5-bisphosphate hydrolyzing activity in vivo, while phosphorylation does not affect the catalytic activity in vitro. Tyrosine 153-156 phospholipase C gamma 1 Homo sapiens 165-174 9716455-3 1998 Tyr-783-phosphorylated PLCgamma1 was not detected in the absence of PDGF, appeared after stimulation, increased for 30 min, and then decreased to near the prestimulation level. Tyrosine 0-3 phospholipase C gamma 1 Homo sapiens 23-32 9716455-4 1998 Immunostaining of cells showed that PDGF-produced Tyr-783-phosphorylated PLCgamma1 localized predominantly at membrane ruffles and stress fibers where it colocalized with actin filaments within 30 min. Tyrosine 50-53 phospholipase C gamma 1 Homo sapiens 73-82 9716455-5 1998 Ninety minutes after PDGF stimulation, the actin filaments were disassembled to short fragments, and the levels of Tyr-783-phosphorylated PLCgamma1 were remarkably decreased in membrane ruffles and cytoskeleton. Tyrosine 115-118 phospholipase C gamma 1 Homo sapiens 138-147 9716455-8 1998 These data suggest that the phosphorylation of PLCgamma1 on tyrosine 783 by PDGF plays an important role in cytoskeletal reorganization in addition to mitogenesis. Tyrosine 60-68 phospholipase C gamma 1 Homo sapiens 47-56 9647226-4 1998 One such substrate, phospholipase C (PLC)-gamma1, becomes tyrosine phosphorylated on CD3/TCR activation and mediates inositol triphosphate-dependent Ca2+ flux. Tyrosine 58-66 phospholipase C gamma 1 Homo sapiens 20-48 9647226-5 1998 Co-cross-linking of T cells with anti-CD3 and anti-V7 resulted in selective inhibition of PLC-gamma1 tyrosine phosphorylation, which may explain V7-mediated blockade of anti-CD3-induced Ca2+ flux. Tyrosine 101-109 phospholipase C gamma 1 Homo sapiens 90-100 9600070-5 1998 Furthermore, stimulation of B2 receptors in these cells is accompanied by a transient tyrosine phosphorylation of PLC gamma 1. Tyrosine 86-94 phospholipase C gamma 1 Homo sapiens 114-125 9648868-4 1998 Monoamine-activated alpha2M also blocks tyrosine phosphorylation of phospholipase C-gamma1 and extracellular signal-regulated protein kinase (ERK)-1, which are key intracellular proteins involved in trkB signal transduction. Tyrosine 40-48 phospholipase C gamma 1 Homo sapiens 68-90 9516477-1 1998 An early event in signaling by the G-protein-coupled angiotensin II (Ang II) AT1 receptor in vascular smooth muscle cells is the tyrosine phosphorylation and activation of phospholipase Cgamma1 (PLCgamma1). Tyrosine 129-137 phospholipase C gamma 1 Homo sapiens 195-204 9529333-4 1998 When expressed in 293T human fibroblast cells and tyrosine-phosphorylated, pp36 associated with phospholipase Cgamma-1 and Grb2. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 96-118 9516477-2 1998 In the present study, we show that stimulation of this event by Ang II in vascular smooth muscle cells is accompanied by binding of PLCgamma1 to the AT1 receptor in an Ang II- and tyrosine phophorylation-dependent manner. Tyrosine 180-188 phospholipase C gamma 1 Homo sapiens 132-141 9516477-3 1998 The PLCgamma1-AT1 receptor interaction appears to depend on phosphorylation of tyrosine 319 in a YIPP motif in the C-terminal intracellular domain of the AT1 receptor and binding of the phosphorylated receptor by the most C-terminal of two Src homology 2 domains in PLCgamma1. Tyrosine 79-87 phospholipase C gamma 1 Homo sapiens 4-13 9516477-3 1998 The PLCgamma1-AT1 receptor interaction appears to depend on phosphorylation of tyrosine 319 in a YIPP motif in the C-terminal intracellular domain of the AT1 receptor and binding of the phosphorylated receptor by the most C-terminal of two Src homology 2 domains in PLCgamma1. Tyrosine 79-87 phospholipase C gamma 1 Homo sapiens 266-275 9489702-2 1998 Here we report the cloning of the cDNA for a highly tyrosine-phosphorylated 36-38 kDa protein, previously characterized by its association with Grb2, phospholipase C-gamma1, and the p85 subunit of phosphoinositide 3-kinase. Tyrosine 52-60 phospholipase C gamma 1 Homo sapiens 150-172 9570517-0 1998 The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 97-105 phospholipase C gamma 1 Homo sapiens 44-67 9570517-0 1998 The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 97-105 phospholipase C gamma 1 Homo sapiens 125-148 9570517-1 1998 TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism. Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 25-48 9570517-1 1998 TCR engagement activates phospholipase C gamma 1 (PLC gamma 1) via a tyrosine phosphorylation-dependent mechanism. Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 50-61 9570517-2 1998 PLC gamma 1 contains a pair of Src homology 2 (SH2) domains whose function is that of promoting protein interactions by binding phosphorylated tyrosine and adjacent amino acids. Tyrosine 143-151 phospholipase C gamma 1 Homo sapiens 0-11 9570517-4 1998 Mutation of the amino-terminal SH2 domain (SH2(N) domain) resulted in defective tyrosine phosphorylation of PLC gamma 1 in response to TCR/CD3 perturbation. Tyrosine 80-88 phospholipase C gamma 1 Homo sapiens 108-119 9570517-8 1998 In contrast to TCR/CD3 ligation, treatment of cells with pervanadate induced tyrosine phosphorylation of either PLC gamma 1 SH2(N) or SH2(C) domain mutants to a level comparable with that of the wild-type protein, indicating that pervanadate treatment induces an alternate mechanism of PLC gamma 1 phosphorylation. Tyrosine 77-85 phospholipase C gamma 1 Homo sapiens 112-123 9281317-3 1997 Inhibition of PLC-gamma1 tyrosine phosphorylation by phenylarsine oxide reduces the co-immunoprecipitation of PLC-gamma1 with GRB2. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 14-24 9356485-4 1997 As a consequence, tyrosine phosphorylation of phospholipase C-gamma1, generation of inositol phosphates, release of arachidonic acid, and secretion of histamine and tumor necrosis factor alpha were also inhibited. Tyrosine 18-26 phospholipase C gamma 1 Homo sapiens 46-68 9281317-3 1997 Inhibition of PLC-gamma1 tyrosine phosphorylation by phenylarsine oxide reduces the co-immunoprecipitation of PLC-gamma1 with GRB2. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 110-120 9281317-4 1997 Furthermore, angiotensin II, a G protein-coupled receptor agonist, also induces the tyrosine phosphorylation of PLC-gamma1 and its co-immunoprecipitation with GRB2 in WB cells. Tyrosine 84-92 phospholipase C gamma 1 Homo sapiens 112-122 9281317-5 1997 Interestingly, angiotensin II stimulation also causes tyrosine phosphorylation of the EGF receptor, suggesting that angiotensin II-induced PLC-gamma1 tyrosine phosphorylation in WB cells may be via EGF receptor tyrosine kinase activation. Tyrosine 54-62 phospholipase C gamma 1 Homo sapiens 139-149 9281317-5 1997 Interestingly, angiotensin II stimulation also causes tyrosine phosphorylation of the EGF receptor, suggesting that angiotensin II-induced PLC-gamma1 tyrosine phosphorylation in WB cells may be via EGF receptor tyrosine kinase activation. Tyrosine 150-158 phospholipase C gamma 1 Homo sapiens 139-149 9281317-7 1997 In vitro studies further demonstrate that the Tyr771 and Tyr783 region of PLC-gamma1 and the SH2 domain of GRB2 are potentially involved in the tyrosine phosphorylation-dependent association between PLC-gamma1 and GRB2. Tyrosine 144-152 phospholipase C gamma 1 Homo sapiens 74-84 9281317-7 1997 In vitro studies further demonstrate that the Tyr771 and Tyr783 region of PLC-gamma1 and the SH2 domain of GRB2 are potentially involved in the tyrosine phosphorylation-dependent association between PLC-gamma1 and GRB2. Tyrosine 144-152 phospholipase C gamma 1 Homo sapiens 199-209 9293962-5 1997 The bradykinin-induced tyrosine phosphorylation of PLC-gamma1 was relatively transient and was associated with an increase in intracellular levels of IP3. Tyrosine 23-31 phospholipase C gamma 1 Homo sapiens 51-61 9164868-8 1997 Although PLCgamma1 is tyrosine phosphorylated in response to many agonists, we could not detect, by Western analysis with anti-phosphotyrosine antibodies, tyrosine phosphorylation of PLCgamma1 immunoprecipitated from thrombin-stimulated platelets. Tyrosine 22-30 phospholipase C gamma 1 Homo sapiens 9-18 9200455-1 1997 CD38 ligation with the specific mAb IB4 induced early and late signaling events in Jurkat T cells, as judged by the transient induction of tyrosine phosphorylation of phospholipase C-gamma1, c-Cbl, zeta-associated protein (ZAP)-70, Shc, extracellular signal-regulated protein kinase-2 (Erk-2) as mitogen-activated protein (MAP) kinase, and increased expression of the activation Ag CD69. Tyrosine 139-147 phospholipase C gamma 1 Homo sapiens 167-189 9079813-4 1997 Results demonstrate that in BW5147 wild-type TCR, tail-less zeta TCR, CD3epsilon, and TCRzeta transduce signals leading to tyrosine phosphorylation of similar sets of cellular substrates, including the receptor subunits, Fyn, ZAP-70, and phospholipase Cgamma1 (PLCgamma1). Tyrosine 123-131 phospholipase C gamma 1 Homo sapiens 238-259 9079813-4 1997 Results demonstrate that in BW5147 wild-type TCR, tail-less zeta TCR, CD3epsilon, and TCRzeta transduce signals leading to tyrosine phosphorylation of similar sets of cellular substrates, including the receptor subunits, Fyn, ZAP-70, and phospholipase Cgamma1 (PLCgamma1). Tyrosine 123-131 phospholipase C gamma 1 Homo sapiens 261-270 9079813-6 1997 These data indicate that tyrosine phosphorylation of PLCgamma1 is not sufficient to drive IP3 production and [Ca2+]i mobilization. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 53-62 9020117-3 1997 By using a glutathione S-transferase fusion protein containing the src homology 2 domains of phospholipase C-gamma1 to specifically recognize tyrosine 992 on the EGF receptor (Tyr(P)992), we have found differences in this subpopulation of receptors. Tyrosine 142-150 phospholipase C gamma 1 Homo sapiens 93-115 9020117-3 1997 By using a glutathione S-transferase fusion protein containing the src homology 2 domains of phospholipase C-gamma1 to specifically recognize tyrosine 992 on the EGF receptor (Tyr(P)992), we have found differences in this subpopulation of receptors. Tyrosine 176-179 phospholipase C gamma 1 Homo sapiens 93-115 9252243-3 1997 We show that TGF-beta1 suppresses PDGF-stimulated tyrosine phosphorylation of PLC-gamma1, and the phosphorylation of Erk. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 78-88 9029091-6 1997 Surprisingly, however, TCR-mediated tyrosine phosphorylation of phospholipase C gamma 1 remains intact in the Jurkat cells expressing the A2/HCP chimera. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 64-87 9081683-2 1997 Endothelial cells responded to pervanadate treatment by increasing tyrosine phosphorylation of cellular proteins, including phospholipase C (PLC) gamma 1, generating inositol phosphates (IPs), releasing arachidonic acid, and producing prostacyclin (prostaglandin [PG] I2). Tyrosine 67-75 phospholipase C gamma 1 Homo sapiens 124-153 9081683-8 1997 While the tyrosine phosphorylation of PLC gamma 1 was enhanced after cotreatment with thrombin and pervanadate compared with pervanadate alone, costimulation with pervanadate and histamine resulted in no more tyrosine phosphorylation of PLC gamma 1 than after pervanadate alone. Tyrosine 10-18 phospholipase C gamma 1 Homo sapiens 38-49 9081683-13 1997 Moreover, thrombin- but not histamine-induced generation of IPs appears to be partly caused by tyrosine phosphorylation of PLC gamma 1. Tyrosine 95-103 phospholipase C gamma 1 Homo sapiens 123-134 8977179-6 1997 Tyrosine phosphorylation of PLCgamma1, induced by CD3 activation, was not affected, but its association with tyrosine-phosphorylated proteins, including a 62-kDa protein, was disrupted. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 28-37 8977179-6 1997 Tyrosine phosphorylation of PLCgamma1, induced by CD3 activation, was not affected, but its association with tyrosine-phosphorylated proteins, including a 62-kDa protein, was disrupted. Tyrosine 109-117 phospholipase C gamma 1 Homo sapiens 28-37 8906806-8 1996 By contrast, CD2 induces PLCgamma-1 tyrosine phosphorylation as efficiently as CD3, with a correlated inositol phosphate production and intracellular calcium increase, and even a higher production of IL-2. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 25-35 8943348-1 1996 Following binding of platelet-derived growth factor (PDGF), the PDGF alpha receptor (alphaPDGFR) becomes tyrosine phosphorylated and associates with a number of signal transduction molecules, including phospholipase Cgamma-1 (PLCgamma-1), phosphatidylinositol 3-kinase (PI3K), the phosphotyrosine phosphatase SHP-2, Grb2, and Src. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 226-236 8951035-7 1996 One of the platelet proteins phosphorylated on tyrosine residues in response to ALPA was found to be PLC-gamma1. Tyrosine 47-55 phospholipase C gamma 1 Homo sapiens 101-111 8951035-10 1996 Upon stimulation of platelets, ALPA induces the activation of phospholipases A2 and C, and tyrosine phosphorylation of several cellular proteins including PLC-gamma1. Tyrosine 91-99 phospholipase C gamma 1 Homo sapiens 155-165 8906806-9 1996 Interestingly, the SH2 domains of PLCgamma-1 associate with ZAP-70 upon CD3 stimulation while they bind, in CD2-activated cells, to a heavily tyrosine-phosphorylated 62-kDa protein. Tyrosine 142-150 phospholipase C gamma 1 Homo sapiens 34-44 8626561-8 1996 These interactions were specific as molecules known to be tyrosine-phosphorylated following TcR cross-linking, phospholipase C-gamma1 and Fyn, were not bound. Tyrosine 58-66 phospholipase C gamma 1 Homo sapiens 111-133 8831704-0 1996 Beta 1 integrin ligation stimulates tyrosine phosphorylation of phospholipase C gamma 1 and elevates intracellular Ca2+ in pancreatic acinar cells. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 64-87 8831704-6 1996 This led us to investigate phospholipase C gamma 1 (PLC gamma 1), a key enzyme responsible for diacylglycerol generation, as a target for integrin-mediated TYR phosphorylation. Tyrosine 156-159 phospholipase C gamma 1 Homo sapiens 27-50 8798459-6 1996 Thus, total deletion of the cytoplasmic tail of FcgammaRIIIAalpha results in a severely impaired tyrosine phosphorylation of phospholipase C-gamma1, zap, and syk and rise in intracellular free Ca2+ following receptor ligation with specific anti-CD16 monoclonal antibody or Ig-anti-Ig complexes, suggesting that FcgammaRIIIAalpha-zeta association per se is not sufficient to establish the signal function of FcgammaRIIIA. Tyrosine 97-105 phospholipase C gamma 1 Homo sapiens 125-147 8649391-0 1996 Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C gamma 1 activation in T cells. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 69-92 8649391-4 1996 Interestingly, TCR ligation of the transfected cells also fails to induce soluble inositol phosphate production and intracellular calcium mobilization, although receptor-mediated tyrosine phosphorylation of phospholipase C gamma 1 still occurs. Tyrosine 179-187 phospholipase C gamma 1 Homo sapiens 207-230 8649391-6 1996 These data demonstrate that tyrosine phosphorylation of a protein(s) which binds the SH2 domain of Grb2 correlates with phospholipase C gamma 1 activation and suggest that such a phosphoprotein(s) plays a critical role in coupling the TCR with the phosphatidylinositol second-messenger pathway. Tyrosine 28-36 phospholipase C gamma 1 Homo sapiens 120-143 8645211-6 1996 In accordance with this, we also found that both the LTD4-induced formation of inositol 1,4,5-trisphosphate and the LTD4-induced phosphorylation of phospholipase C gamma 1 (PLC gamma 1) on tyrosine residues were significantly reduced in compactin-pretreated cells. Tyrosine 189-197 phospholipase C gamma 1 Homo sapiens 148-171 8645211-6 1996 In accordance with this, we also found that both the LTD4-induced formation of inositol 1,4,5-trisphosphate and the LTD4-induced phosphorylation of phospholipase C gamma 1 (PLC gamma 1) on tyrosine residues were significantly reduced in compactin-pretreated cells. Tyrosine 189-197 phospholipase C gamma 1 Homo sapiens 173-184 8831704-6 1996 This led us to investigate phospholipase C gamma 1 (PLC gamma 1), a key enzyme responsible for diacylglycerol generation, as a target for integrin-mediated TYR phosphorylation. Tyrosine 156-159 phospholipase C gamma 1 Homo sapiens 52-63 8831704-7 1996 Staining with antiphosphotyrosine antibodies revealed increased TYR phosphorylation of immunoprecipitated PLC gamma 1 prepared from beta 1 integrin-ligated acinar cells. Tyrosine 64-67 phospholipase C gamma 1 Homo sapiens 106-117 8611637-7 1996 Tyrosine-phosphorylation and translocation to the particulate fraction of phospholipase C-gamma 1 (PLC-gamma 1) were observed upon T-cell activation. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 74-97 8786295-7 1996 This inference was further supported by observations that naive T cells from NT animals exhibit tyrosine phosphorylation of several substrates, including phospholipase C-gamma1, which were either absent or underphosphorylated in unstimulated control T cells. Tyrosine 96-104 phospholipase C gamma 1 Homo sapiens 154-176 8621434-5 1996 Both TrkC and TrkA mediate qualitatively similar increases in the tyrosine phosphorylation of phospholipase C (PLC)-gamma1, Shc, SNT, and MAPK and the transcription of the c-fos, c-jun, NGFI-A, and NGFI-B immediate early genes. Tyrosine 66-74 phospholipase C gamma 1 Homo sapiens 94-122 8611637-7 1996 Tyrosine-phosphorylation and translocation to the particulate fraction of phospholipase C-gamma 1 (PLC-gamma 1) were observed upon T-cell activation. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 99-110 8543771-9 1995 One was mediated by enhancement of tyrosine phosphorylation of a 57 kd protein associated with phospholipase C-gamma 1 (PLC-gamma 1) that resulted in PLC-gamma 1 activation, inositol lipid hydrolysis, and protein kinase C delta translocation. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 95-118 8552402-4 1996 While the tyrosine phosphorylation of TrkA, SHC and PLC-gamma 1 increased with time in the presence of NGF and was inhibited by the tyrosine kinase inhibitor K252a, the state of tyrosine phosphorylation of c-Crk-II did not appear to change with NGF treatment. Tyrosine 10-18 phospholipase C gamma 1 Homo sapiens 52-63 8552402-4 1996 While the tyrosine phosphorylation of TrkA, SHC and PLC-gamma 1 increased with time in the presence of NGF and was inhibited by the tyrosine kinase inhibitor K252a, the state of tyrosine phosphorylation of c-Crk-II did not appear to change with NGF treatment. Tyrosine 132-140 phospholipase C gamma 1 Homo sapiens 52-63 8543771-9 1995 One was mediated by enhancement of tyrosine phosphorylation of a 57 kd protein associated with phospholipase C-gamma 1 (PLC-gamma 1) that resulted in PLC-gamma 1 activation, inositol lipid hydrolysis, and protein kinase C delta translocation. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 120-131 8543771-9 1995 One was mediated by enhancement of tyrosine phosphorylation of a 57 kd protein associated with phospholipase C-gamma 1 (PLC-gamma 1) that resulted in PLC-gamma 1 activation, inositol lipid hydrolysis, and protein kinase C delta translocation. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 150-161 7773170-1 1995 Activated epidermal growth factor receptor (EGFR) undergoes autophosphorylation on several cytoplasmic tyrosine residues, which may then associate with the src homology-2 (SH2) domains of effector proteins such as phospholipase C gamma-1 (PLC gamma-1). Tyrosine 103-111 phospholipase C gamma 1 Homo sapiens 214-237 7594525-3 1995 It also induces in parallel the early tyrosine phosphorylation of numerous proteins, including phospholipase C gamma-1. Tyrosine 38-46 phospholipase C gamma 1 Homo sapiens 95-118 8525617-5 1995 Phosphopeptide analysis indicated that the phosphorylation of the PLC-gamma 1 by VGF includes tyrosine residues identical to those phosphorylated by EGF. Tyrosine 94-102 phospholipase C gamma 1 Homo sapiens 66-77 8525617-6 1995 These results suggest that tyrosine phosphorylation of PLC-gamma 1, mediated by VGF, leads to activation of PLC-gamma 1 and a concomitant increase in phosphatidylinositol turnover. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 55-66 8525617-6 1995 These results suggest that tyrosine phosphorylation of PLC-gamma 1, mediated by VGF, leads to activation of PLC-gamma 1 and a concomitant increase in phosphatidylinositol turnover. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 108-119 7487955-5 1995 Tyrosine phosphorylation of PLC gamma 1 correlated with the time- and concentration-dependent decrease in the mass of membrane phosphatidylinositol 4,5-bisphosphate (PIP2) and the increase in the epithelial concentration of inositol 1,4,5-trisphosphate (IP3). Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 28-39 7822789-3 1995 Recently, PLC gamma 1 has been shown to be tyrosine phosphorylated in T cells after receptor activation. Tyrosine 43-51 phospholipase C gamma 1 Homo sapiens 10-21 8525617-3 1995 We found tyrosine-phosphorylations of PLC-gamma 1 and concomitant increase of the phosphoinositides level in the human epidermoidal A431 cells either treated with purified VGF or infected with vaccinia virus. Tyrosine 9-17 phospholipase C gamma 1 Homo sapiens 38-49 7487955-3 1995 In this study, we demonstrate a novel feature of the action of gastrin on normal colonic cells, namely the rapid phosphorylation on tyrosine of phospholipase C gamma 1 (PLC gamma 1). Tyrosine 132-140 phospholipase C gamma 1 Homo sapiens 144-167 7487955-3 1995 In this study, we demonstrate a novel feature of the action of gastrin on normal colonic cells, namely the rapid phosphorylation on tyrosine of phospholipase C gamma 1 (PLC gamma 1). Tyrosine 132-140 phospholipase C gamma 1 Homo sapiens 169-180 7487955-4 1995 Tyrosine phosphorylation of PLC gamma 1, elicited by gastrin, was transient, concentration-dependent, and was abrogated by pretreating the colonic cells with the gastrin-receptor antagonist proglumide, the tyrosine kinase inhibitor genistein, and by removal of the tyrosine phosphatase inhibitor orthovanadate from the isolation buffer. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 28-39 7628642-3 1995 PAO (1 microM) also inhibited completely tyrosine phosphorylation of PLC gamma 1 induced by platelet derived growth factor (PDGF) in NIH-3T3 fibroblasts but only partially reduced phosphorylation of the PDGF receptor. Tyrosine 41-49 phospholipase C gamma 1 Homo sapiens 69-80 7790382-5 1995 Further studies show that PDGF-induced tyrosine phosphorylation of phospholipase C-gamma 1 (PLC-gamma 1) and phosphatidylinositol 3-kinase (PI 3-kinase) are also suppressed in dibutyryl-cAMP-pretreated cells. Tyrosine 39-47 phospholipase C gamma 1 Homo sapiens 67-90 7790382-5 1995 Further studies show that PDGF-induced tyrosine phosphorylation of phospholipase C-gamma 1 (PLC-gamma 1) and phosphatidylinositol 3-kinase (PI 3-kinase) are also suppressed in dibutyryl-cAMP-pretreated cells. Tyrosine 39-47 phospholipase C gamma 1 Homo sapiens 92-103 7790382-6 1995 The suppression of PLC-gamma 1 tyrosine phosphorylation was accompanied by a decreased production of water soluble inositol phosphates. Tyrosine 31-39 phospholipase C gamma 1 Homo sapiens 19-30 7790382-7 1995 In contrast, similar treatment with normal human astrocytes potentiates the tyrosine phosphorylation of PLC-gamma 1 and PI 3-kinase. Tyrosine 76-84 phospholipase C gamma 1 Homo sapiens 104-115 7529791-5 1995 Furthermore, MHC-I cross-linking was shown to tyrosine phosphorylate PLC-gamma 1 (phospholipase C-gamma 1). Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 69-105 7773170-1 1995 Activated epidermal growth factor receptor (EGFR) undergoes autophosphorylation on several cytoplasmic tyrosine residues, which may then associate with the src homology-2 (SH2) domains of effector proteins such as phospholipase C gamma-1 (PLC gamma-1). Tyrosine 103-111 phospholipase C gamma 1 Homo sapiens 239-250 7523557-4 1994 In addition, such coengagement stimulated TCR-dependent activation and tyrosine phosphorylation of phospholipase C gamma 1 (PLC gamma 1). Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 99-122 7989748-4 1994 Anti-phosphotyrosine immunoprecipitates from lysates of PAF-stimulated cells, when fractionated by SDS-PAGE and analyzed by Western blotting with anti-PLC-gamma 1, showed that maximal tyrosine phosphorylation of this enzyme occurred within 2 min of stimulation. Tyrosine 12-20 phospholipase C gamma 1 Homo sapiens 151-162 7989748-8 1994 We have thus demonstrated that the activation of tyrosine kinases is an important proximate step in PAF-mediated signal transduction in B cells, leading to tyrosine phosphorylation and activation of PLC-gamma 1, Fyn and Lyn kinases, and PtdIns 3-kinase. Tyrosine 49-57 phospholipase C gamma 1 Homo sapiens 199-210 7937868-2 1994 Crosslinking Fc gamma RIIA with anti-Fc gamma RII monoclonal antibody also induced tyrosine phosphorylation of multiple proteins including Fc gamma RIIA, ZAP-70, p72SYK, and phospholipase C gamma 1 subunit and an increase in intracellular Ca2+ concentration. Tyrosine 83-91 phospholipase C gamma 1 Homo sapiens 174-197 7523557-4 1994 In addition, such coengagement stimulated TCR-dependent activation and tyrosine phosphorylation of phospholipase C gamma 1 (PLC gamma 1). Tyrosine 71-79 phospholipase C gamma 1 Homo sapiens 124-135 8132732-4 1994 Subsequent events include phosphorylation on tyrosine of multiple cellular substrates including phospholipase C gamma 1 and PI3-kinase. Tyrosine 45-53 phospholipase C gamma 1 Homo sapiens 96-119 7999363-10 1994 We propose that phosphorylation of tyr-766, which is required for interaction of phospholipase C gamma 1 (PLC gamma 1) with the receptor, may occur by a cis-intramolecular mechanism within FGFR monomers, while phosphorylation of tyr-653, which is required for phosphorylation of PLC gamma 1, may occur by a trans-intermolecular mechanism between monomers within kinase homodimers. Tyrosine 35-38 phospholipase C gamma 1 Homo sapiens 81-104 7999363-10 1994 We propose that phosphorylation of tyr-766, which is required for interaction of phospholipase C gamma 1 (PLC gamma 1) with the receptor, may occur by a cis-intramolecular mechanism within FGFR monomers, while phosphorylation of tyr-653, which is required for phosphorylation of PLC gamma 1, may occur by a trans-intermolecular mechanism between monomers within kinase homodimers. Tyrosine 35-38 phospholipase C gamma 1 Homo sapiens 106-117 7999363-10 1994 We propose that phosphorylation of tyr-766, which is required for interaction of phospholipase C gamma 1 (PLC gamma 1) with the receptor, may occur by a cis-intramolecular mechanism within FGFR monomers, while phosphorylation of tyr-653, which is required for phosphorylation of PLC gamma 1, may occur by a trans-intermolecular mechanism between monomers within kinase homodimers. Tyrosine 35-38 phospholipase C gamma 1 Homo sapiens 279-290 7999363-10 1994 We propose that phosphorylation of tyr-766, which is required for interaction of phospholipase C gamma 1 (PLC gamma 1) with the receptor, may occur by a cis-intramolecular mechanism within FGFR monomers, while phosphorylation of tyr-653, which is required for phosphorylation of PLC gamma 1, may occur by a trans-intermolecular mechanism between monomers within kinase homodimers. Tyrosine 229-232 phospholipase C gamma 1 Homo sapiens 81-104 7999363-10 1994 We propose that phosphorylation of tyr-766, which is required for interaction of phospholipase C gamma 1 (PLC gamma 1) with the receptor, may occur by a cis-intramolecular mechanism within FGFR monomers, while phosphorylation of tyr-653, which is required for phosphorylation of PLC gamma 1, may occur by a trans-intermolecular mechanism between monomers within kinase homodimers. Tyrosine 229-232 phospholipase C gamma 1 Homo sapiens 106-117 8036006-3 1994 In transfected NIH3T3 cells expressing human EGF receptors (approximately 4 x 10(5) receptors per cell), maximal levels of SHC and PLC-gamma 1 tyrosine phosphorylation occur when approximately 4 x 10(4) receptors or more are occupied by ligand. Tyrosine 143-151 phospholipase C gamma 1 Homo sapiens 131-142 8208538-2 1994 In this study we examine the ability of tyrosine phosphorylated proteins from Jurkat T cells stimulated by CD2 or T cell receptor-CD3 to interact with the src homology 2 or src homology 3 domains from eight different proteins involved in signal transduction in lymphocytes: Vav, Shc, Nck, phosphatidylinositol-3-kinase, phospholipase C-gamma 1, Ras-GTPase activating protein, c-Crk and Grb2. Tyrosine 40-48 phospholipase C gamma 1 Homo sapiens 320-343 7511641-7 1994 Accordingly, tyrosine phosphorylation of PLC gamma-1 can be evidenced but only in Jurkat cells highly expressing GM1. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 41-52 8144900-3 1994 In addition, tyrosine phosphorylated Fc gamma RIIA was co-precipitated with activated PLC-gamma 1. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 86-97 8034732-4 1994 We showed that the tyrosine phosphorylated 145- kDa protein is identical to phospholipase C-gamma 1 (PLC-gamma 1). Tyrosine 19-27 phospholipase C gamma 1 Homo sapiens 76-99 8034732-4 1994 We showed that the tyrosine phosphorylated 145- kDa protein is identical to phospholipase C-gamma 1 (PLC-gamma 1). Tyrosine 19-27 phospholipase C gamma 1 Homo sapiens 101-112 8034732-7 1994 Additionally, in Epo-stimulated cells, PLC-gamma 1 become physically associated with 80- and 40-kDa proteins which have been tyrosine-phosphorylated in response to Epo. Tyrosine 125-133 phospholipase C gamma 1 Homo sapiens 39-50 8144900-7 1994 These results suggest that tyrosine phosphorylation of Shc and PLC-gamma 1 is important for the initiation of [Ca2+]i flux, and that activation of protein kinase C may modulate the activity of PLC-gamma 1 through serine/threonine phosphorylation. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 63-74 8144900-7 1994 These results suggest that tyrosine phosphorylation of Shc and PLC-gamma 1 is important for the initiation of [Ca2+]i flux, and that activation of protein kinase C may modulate the activity of PLC-gamma 1 through serine/threonine phosphorylation. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 193-204 7693851-0 1993 Tyrosine phosphorylation and association with phospholipase C gamma-1 of the GAP-associated 62-kD protein after CD2 stimulation of Jurkat T cell. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 46-69 7693695-3 1993 Simultaneous stimulation of T cells with anti-CD3 monoclonal antibody and phenylarsine oxide prevented increased tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 113-121 phospholipase C gamma 1 Homo sapiens 141-164 8225779-3 1993 Peptide 1, derived from the Tyr 992 site, inhibited binding of a 35S-labelled fusion protein containing both of the SH2 domains from PLC gamma 1 to the phosphorylated EGFR with an IC50 of 8 microM. Tyrosine 28-31 phospholipase C gamma 1 Homo sapiens 133-144 7689859-5 1993 Previously, it had been shown that PLC-gamma 1 was phosphorylated on tyrosine residues by the agonist-occupied platelet-derived growth factor (PDGF) receptor and epidermal growth factor (EGF) receptor in cells other than platelets. Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 35-46 8321198-11 1993 Although phosphotyrosine 766 is sufficient for interaction of PLC gamma 1 and other SH2 substrates with the FGF-R kinase, phosphorylation and presumably activation of substrates require the kinase homodimer and phosphorylation of Tyr-653. Tyrosine 230-233 phospholipase C gamma 1 Homo sapiens 62-73 8353285-6 1993 The synergistic induction of tyrosine phosphorylation by H2O2 plus vanadate included physiologically relevant proteins such as PLC gamma 1. Tyrosine 29-37 phospholipase C gamma 1 Homo sapiens 127-138 8353285-9 1993 Induction of tyrosine phosphorylation by ROI may thus lead to many of the pleiotropic effects of ROI in lymphoid cells, including downstream activation of PLC gamma 1 and NF-kappa B. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 155-166 8327490-6 1993 The rapid rise in intracellular Ca2+ induced by DMBA alone was accompanied by a rapid but transient increase in inositol 1,4,5-trisphosphate and tyrosine phosphorylation of phospholipase C-gamma 1. Tyrosine 145-153 phospholipase C gamma 1 Homo sapiens 173-196 8327490-9 1993 The mechanism of DMBA-induced tyrosine phosphorylation of phospholipase C-gamma 1 may have been due to an increase in protein-tyrosine kinase activity, since it was found that DMBA produced a > 2-fold increase in the activity of the T-cell receptor-associated Src-family kinases Fyn and Lck. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 58-81 8327490-11 1993 Thus, it is likely that the Fyn kinase or other protein-tyrosine kinases may be responsible for the early tyrosine phosphorylation of phospholipase C-gamma 1, which results in inositol 1,4,5-trisphosphate release and mobilization of intracellular Ca2+. Tyrosine 56-64 phospholipase C gamma 1 Homo sapiens 134-157 8334306-6 1993 Phospholipase C (PLC) gamma 1 was tyrosine phosphorylated in response to UV irradiation but to a lesser extent than observed after CD3 cross-linking. Tyrosine 34-42 phospholipase C gamma 1 Homo sapiens 0-29 8515060-6 1993 As expected, activation of IL-2R by IL-2 induced tyrosine phosphorylation of several proteins including p56lck, and class II cross-linking by mAb induced tyrosine phosphorylation of specific substrates including PLC-gamma 1. Tyrosine 49-57 phospholipase C gamma 1 Homo sapiens 212-223 8515060-6 1993 As expected, activation of IL-2R by IL-2 induced tyrosine phosphorylation of several proteins including p56lck, and class II cross-linking by mAb induced tyrosine phosphorylation of specific substrates including PLC-gamma 1. Tyrosine 154-162 phospholipase C gamma 1 Homo sapiens 212-223 8391259-7 1993 Our results provide the first evidence for a direct or indirect regulation of PtdIns(3,4)P2 accumulation and PLC gamma 1 activity by tyrosine phosphorylation during thrombin stimulation of human platelets. Tyrosine 133-141 phospholipase C gamma 1 Homo sapiens 109-120 8334306-7 1993 However, PLC gamma 1-associated proteins demonstrated to bind to the PLC gamma 1 SH2 domain were tyrosine phosphorylated strongly after UV irradiation. Tyrosine 97-105 phospholipase C gamma 1 Homo sapiens 9-20 8334306-7 1993 However, PLC gamma 1-associated proteins demonstrated to bind to the PLC gamma 1 SH2 domain were tyrosine phosphorylated strongly after UV irradiation. Tyrosine 97-105 phospholipase C gamma 1 Homo sapiens 69-80 8334306-8 1993 A similar dose response was observed for the inhibition by herbimycin A of UV-induced calcium signals and UV-induced tyrosine phosphorylation of PLC gamma 1 and associated proteins. Tyrosine 117-125 phospholipase C gamma 1 Homo sapiens 145-156 8454849-0 1993 Cross-linking of Fc gamma RIIIA on natural killer cells results in tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2. Tyrosine 67-75 phospholipase C gamma 1 Homo sapiens 95-122 8454849-4 1993 Cross-linking of Fc gamma RIIIA on NK3.3 cells induced a rapid phosphorylation of PLC-gamma 1 and PLC-gamma 2 on tyrosine residues. Tyrosine 113-121 phospholipase C gamma 1 Homo sapiens 82-93 8454849-5 1993 Pretreatment of NK3.3 cells with a tyrosine kinase inhibitor, herbimycin A, prevented the tyrosine phosphorylation of both PLC-gamma 1 and PLC-gamma 2. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 123-134 8452536-3 1993 In support of this, peroxovanadate stimulates tyrosine phosphorylation of phospholipase C gamma 1, suggesting that this may underlie its mechanism of platelet activation. Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 74-97 7679423-2 1993 Because phosphorylation of phospholipase C-gamma 1 on tyrosine residues is known to be involved in the activation of phosphatidylinositide turnover, we investigated the role of tyrosine protein kinase (TPK) in the signal transduction for IFN-gamma-inducible DR molecule expression on T98G cells. Tyrosine 54-62 phospholipase C gamma 1 Homo sapiens 27-50 8470127-5 1993 The results show a CDNB dose-dependent reduction in GSH content, the magnitude of intracellular free calcium mobilization, and the extent of tyrosine phosphorylation of several proteins, including phospholipase C-gamma 1. Tyrosine 141-149 phospholipase C gamma 1 Homo sapiens 197-220 8443409-3 1993 Mutation of Tyr 1021 markedly reduced the PDGF-stimulated binding of phospholipase C (PLC) gamma 1 but had no effect on binding of the GTPase activator protein of Ras or of phosphatidylinositol 3 kinase. Tyrosine 12-15 phospholipase C gamma 1 Homo sapiens 69-98 8443409-5 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, also reduced the PDGF-dependent binding of a transiently expressed fusion protein containing the two Src-homology 2 domains from PLC gamma 1. Tyrosine 12-15 phospholipase C gamma 1 Homo sapiens 182-193 8386518-8 1993 CD28 receptor ligation induces tyrosine phosphorylation of specific substrates, including phospholipase C gamma 1, and triggers both calcium-dependent and calcium-independent signals. Tyrosine 31-39 phospholipase C gamma 1 Homo sapiens 90-113 8443409-5 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, also reduced the PDGF-dependent binding of a transiently expressed fusion protein containing the two Src-homology 2 domains from PLC gamma 1. Tyrosine 30-33 phospholipase C gamma 1 Homo sapiens 182-193 8443409-4 1993 Mutation of Tyr 1009 reduced binding of PLC gamma 1 less severely. Tyrosine 12-15 phospholipase C gamma 1 Homo sapiens 40-51 8443409-5 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, also reduced the PDGF-dependent binding of a transiently expressed fusion protein containing the two Src-homology 2 domains from PLC gamma 1. Tyrosine 30-33 phospholipase C gamma 1 Homo sapiens 182-193 8443409-6 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, greatly reduced PDGF-stimulated tyrosine phosphorylation of PLC gamma 1 but did not prevent the tyrosine phosphorylation of other cell proteins, including mitogen-activated protein kinase. Tyrosine 12-15 phospholipase C gamma 1 Homo sapiens 113-124 1500851-1 1992 Stimulation of the T cell antigen receptor (TCR) activates a protein tyrosine kinase and leads to the tyrosine phosphorylation of phosphoinositide-specific phospholipase C-gamma 1 (PLC gamma 1). Tyrosine 69-77 phospholipase C gamma 1 Homo sapiens 181-192 8443409-6 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, greatly reduced PDGF-stimulated tyrosine phosphorylation of PLC gamma 1 but did not prevent the tyrosine phosphorylation of other cell proteins, including mitogen-activated protein kinase. Tyrosine 30-33 phospholipase C gamma 1 Homo sapiens 113-124 8443409-6 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, greatly reduced PDGF-stimulated tyrosine phosphorylation of PLC gamma 1 but did not prevent the tyrosine phosphorylation of other cell proteins, including mitogen-activated protein kinase. Tyrosine 30-33 phospholipase C gamma 1 Homo sapiens 113-124 8443409-6 1993 Mutation of Tyr 1021, or both Tyr 1009 and Tyr 1021, greatly reduced PDGF-stimulated tyrosine phosphorylation of PLC gamma 1 but did not prevent the tyrosine phosphorylation of other cell proteins, including mitogen-activated protein kinase. Tyrosine 85-93 phospholipase C gamma 1 Homo sapiens 113-124 8443409-7 1993 We conclude that Tyr 1021, and possibly Tyr 1009, is a binding site for PLC gamma 1. Tyrosine 17-20 phospholipase C gamma 1 Homo sapiens 72-83 8443409-7 1993 We conclude that Tyr 1021, and possibly Tyr 1009, is a binding site for PLC gamma 1. Tyrosine 40-43 phospholipase C gamma 1 Homo sapiens 72-83 1385526-3 1992 Both types of stimuli induced tyrosine phosphorylation of phosphatidylinositol-specific phospholipase C gamma 1 (PLC gamma 1) and an increase in intracellular calcium concentration; however, superantigen-induced signaling was stronger than class II ligation alone. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 58-124 1438211-4 1992 Cross-linking of CD3 and CD22 T-cell ligands with anti-CD3 antibody and soluble CD22 is shown to block anti-CD3-induced intracellular calcium increase and to inhibit tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 166-174 phospholipase C gamma 1 Homo sapiens 194-217 1400471-2 1992 Upon exposure to NGF, a 38-kDa tyrosine-phosphorylated protein (pp38) is identified in both PC-12 pheochromocytoma cells and NIH3T3 cells transfected with the full-length human pp140c-trk cDNA (3T3-c-trk) that is specifically coimmunoprecipitated with pp140c-trk or phosphatidylinositol-phospholipase C (PLC)-gamma 1. Tyrosine 31-39 phospholipase C gamma 1 Homo sapiens 266-316 1281218-0 1992 Fc gamma receptor activation induces the tyrosine phosphorylation of both phospholipase C (PLC)-gamma 1 and PLC-gamma 2 in natural killer cells. Tyrosine 41-49 phospholipase C gamma 1 Homo sapiens 74-103 1281218-6 1992 Furthermore, Fc gamma R crosslinking triggers the tyrosine phosphorylation of both PLC-gamma 1 and PLC-gamma 2 in these cells. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 83-94 1281218-8 1992 Pretreatment with herbimycin A, a PTK inhibitor, blocked the Fc gamma R-induced tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2, and the subsequent release of inositol phosphates. Tyrosine 80-88 phospholipase C gamma 1 Homo sapiens 108-119 1384057-11 1992 Binding of the PLC gamma 1 SH2 fusion protein to a mutant EGF receptor lacking the two carboxyl-terminal tyrosine phosphorylation sites exhibited a significantly lower affinity than that observed with the wild type, suggesting that this region of the receptor may play an important role. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 15-26 1401074-5 1992 As protein tyrosine phosphorylation is thought to represent a proximal event in the activation of B cells, inducing increases in [Ca2+]i by virtue of tyrosine phosphorylation of phospholipase C (PLC)-gamma, profiles of protein tyrosine phosphorylation and expression of tyrosine-phosphorylated PLC-gamma 1 were compared between WAS and normal EBV B cells before and after sIg cross-linking. Tyrosine 11-19 phospholipase C gamma 1 Homo sapiens 294-305 1401074-5 1992 As protein tyrosine phosphorylation is thought to represent a proximal event in the activation of B cells, inducing increases in [Ca2+]i by virtue of tyrosine phosphorylation of phospholipase C (PLC)-gamma, profiles of protein tyrosine phosphorylation and expression of tyrosine-phosphorylated PLC-gamma 1 were compared between WAS and normal EBV B cells before and after sIg cross-linking. Tyrosine 150-158 phospholipase C gamma 1 Homo sapiens 294-305 1401074-5 1992 As protein tyrosine phosphorylation is thought to represent a proximal event in the activation of B cells, inducing increases in [Ca2+]i by virtue of tyrosine phosphorylation of phospholipase C (PLC)-gamma, profiles of protein tyrosine phosphorylation and expression of tyrosine-phosphorylated PLC-gamma 1 were compared between WAS and normal EBV B cells before and after sIg cross-linking. Tyrosine 150-158 phospholipase C gamma 1 Homo sapiens 294-305 1401074-5 1992 As protein tyrosine phosphorylation is thought to represent a proximal event in the activation of B cells, inducing increases in [Ca2+]i by virtue of tyrosine phosphorylation of phospholipase C (PLC)-gamma, profiles of protein tyrosine phosphorylation and expression of tyrosine-phosphorylated PLC-gamma 1 were compared between WAS and normal EBV B cells before and after sIg cross-linking. Tyrosine 150-158 phospholipase C gamma 1 Homo sapiens 294-305 1500851-3 1992 After stimulation of the TCR on Jurkat T cells, tyrosine-phosphorylated proteins of 36, 38, 58, and 63 kD coprecipitate with PLC gamma 1. Tyrosine 48-56 phospholipase C gamma 1 Homo sapiens 125-136 1320023-0 1992 Lymphocyte lineage-restricted tyrosine-phosphorylated proteins that bind PLC gamma 1 SH2 domains. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 73-84 1320023-1 1992 Epidermal growth factor (EGF) or platelet-derived growth factor binding to their receptor on fibroblasts induces tyrosine phosphorylation of PLC gamma 1 and stable association of PLC gamma 1 with the receptor protein tyrosine kinase. Tyrosine 113-121 phospholipase C gamma 1 Homo sapiens 141-152 1320023-4 1992 As in EGF- or platelet-derived growth factor-stimulated fibroblasts, PLC gamma 1 is coprecipitated in activated lymphocytes, complexed with associated tyrosine-phosphorylated proteins. Tyrosine 151-159 phospholipase C gamma 1 Homo sapiens 69-80 1376928-1 1992 The triggering of T- or B-cell antigen-specific receptors is accompanied by rapid tyrosine phosphorylation of distinct cellular substrates, one of which is the gamma 1 isoform of inositol phospholipid-specific phospholipase C (PLC-gamma 1). Tyrosine 82-90 phospholipase C gamma 1 Homo sapiens 227-238 1376928-9 1992 Conversely, and in agreement with recent reports, triggering of the T-cell antigen receptor complex led to the predominant phosphorylation of PLC-gamma 1 on tyrosine. Tyrosine 157-165 phospholipase C gamma 1 Homo sapiens 142-153 1532798-3 1992 In TCR-CD3low cells, in which CD3-zeta was found to be associated with the TCR-CD3 complex, cross-linking CD3 with CD4 resulted in a profile of calcium mobilization, CD3-zeta, and phospholipase C-gamma 1 tyrosine phosphorylation similar to that observed in HPB-ALL cells, although the magnitude of generalized substrate tyrosine phosphorylation appeared to be smaller, as compared with wild-type cells. Tyrosine 204-212 phospholipase C gamma 1 Homo sapiens 180-203 1532798-7 1992 The data also suggest that CD4-associated protein tyrosine kinase p56lck could up-regulate defective CD3-mediated induction of phospholipase C activity by increasing tyrosine phosphorylation of phospholipase C-gamma 1. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 194-217 1372020-0 1992 CD2/LFA-3 ligation induces phospholipase-C gamma 1 tyrosine phosphorylation and regulates CD3 signaling. Tyrosine 51-59 phospholipase C gamma 1 Homo sapiens 27-50 1373507-0 1992 Tyrosine phosphorylation of phospholipase C-gamma 1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgG in U937 cells. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 28-51 1373507-6 1992 Cross-linking of Fc gamma RI or Fc gamma RII resulted in a rapid and transient phosphorylation of PLC-gamma 1 on tyrosine residues. Tyrosine 113-121 phospholipase C gamma 1 Homo sapiens 98-109 1373507-7 1992 It has previously been shown that phosphorylation of PLC-gamma 1 on tyrosine residues activates its enzymatic activity in cells. Tyrosine 68-76 phospholipase C gamma 1 Homo sapiens 53-64 1373507-8 1992 Prior incubation of U937 cells with a protein tyrosine kinase inhibitor, herbimycin A, prevented the tyrosine phosphorylation of PLC-gamma 1 and the hydrolysis of phosphatidylinositol 4,5-bisphosphate induced by the cross-linking of Fc gamma Rs. Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 129-140 1372020-1 1992 Activation of T cells through the TCR/CD3 receptor complex with either specific Ag or antibody results in tyrosine phosphorylation of intracellular protein substrates and phosphatidylinositol-phospholipase C (PLC) signaling, leading to the generation of PI breakdown products and the mobilization of intracellular calcium. Tyrosine 106-114 phospholipase C gamma 1 Homo sapiens 209-212 1372020-3 1992 Previous reports have shown that CD3 activation leads to tyrosine phosphorylation of the PLC isozyme PLC gamma 1. Tyrosine 57-65 phospholipase C gamma 1 Homo sapiens 89-92 1372020-3 1992 Previous reports have shown that CD3 activation leads to tyrosine phosphorylation of the PLC isozyme PLC gamma 1. Tyrosine 57-65 phospholipase C gamma 1 Homo sapiens 101-112 1372020-5 1992 We show that stimulation of CD2 receptors on T cells caused tyrosine phosphorylation of PLC gamma 1. Tyrosine 60-68 phospholipase C gamma 1 Homo sapiens 88-99 1372020-6 1992 Cross-linking of CD2 with CD3 receptors augmented the phosphorylation of PLC gamma 1 on tyrosine, whereas ligation of the CD45 tyrosine phosphatase with CD2 receptors prevented PLC gamma 1 tyrosine phosphorylation. Tyrosine 88-96 phospholipase C gamma 1 Homo sapiens 73-84 1372020-6 1992 Cross-linking of CD2 with CD3 receptors augmented the phosphorylation of PLC gamma 1 on tyrosine, whereas ligation of the CD45 tyrosine phosphatase with CD2 receptors prevented PLC gamma 1 tyrosine phosphorylation. Tyrosine 127-135 phospholipase C gamma 1 Homo sapiens 177-188 1372020-8 1992 Co-ligation of LFA-3/Ig with suboptimal concentrations of anti-CD3 resulted in profound augmentation of PLC gamma 1 tyrosine phosphorylation, mobilization of intracellular calcium and T cell proliferation. Tyrosine 116-124 phospholipase C gamma 1 Homo sapiens 104-115 1372020-10 1992 CD3 receptor modulation potently down-regulated CD2-induced PLC gamma 1 tyrosine phosphorylation and calcium mobilization. Tyrosine 72-80 phospholipase C gamma 1 Homo sapiens 60-71 1386038-0 1992 CD45 regulates TCR-induced signalling through tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 46-54 phospholipase C gamma 1 Homo sapiens 74-97 1550550-6 1992 Immunoprecipitation with antibodies against PLC-gamma 1 or PLC-gamma 2 and subsequent Western blotting with anti-phosphotyrosine antibodies revealed that both PLC-gamma 1 and PLC-gamma 2 are tyrosine phosphorylated in stimulated but not in resting B cells. Tyrosine 120-128 phospholipase C gamma 1 Homo sapiens 159-170 1550550-8 1992 Further, the specific protein tyrosine kinase inhibitors, tyrphostins, which block phospholipase-C activation and proliferation of B cells also inhibited tyrosine phosphorylation on both PLC-gamma 1 and PLC-gamma 2. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 187-198 1544934-4 1992 Herbimycin A, a specific tyrosine kinase inhibitor, both decreases thrombin-induced mitogenesis by greater than 90% and abolishes tyrosine phosphorylation of phospholipase C (PLC)-gamma-1. Tyrosine 25-33 phospholipase C gamma 1 Homo sapiens 158-187 1544934-6 1992 These results provide evidence that herbimycin A specifically inhibits PLC-gamma-1 tyrosine phosphorylation without affecting VSM cell viability or calcium release. Tyrosine 83-91 phospholipase C gamma 1 Homo sapiens 71-82 1532148-5 1992 However, we show here that ligation of CD3 with CD4 leads to tyrosine phosphorylation of PLC gamma 1 and elevation in the intracellular free Ca2+ concentration in CD45- cells that is in excess of that seen in CD45+ cells. Tyrosine 61-69 phospholipase C gamma 1 Homo sapiens 89-100 1371471-9 1992 By immunoprecipitation we found that TcR/CD3 stimulation induced tyrosine phosphorylation of PLC gamma 1, an effect which was enhanced by co-cross-linking CD4 to TcR/CD3. Tyrosine 65-73 phospholipase C gamma 1 Homo sapiens 93-104 1370476-5 1992 These results suggest that the inhibition of PtdIns 4,5-P2 hydrolysis by PMA and cAMP is attributable to reduced tyrosine phosphorylation of PLC-gamma 1. Tyrosine 113-121 phospholipase C gamma 1 Homo sapiens 141-152 1371471-8 1992 Since TcR/CD3 stimulation of mature T cells induces tyrosine phosphorylation of PLC gamma 1, we investigated this phenomenon in thymocytes, and asked whether ligation of CD45 might regulate this process. Tyrosine 52-60 phospholipase C gamma 1 Homo sapiens 80-91 1370476-2 1992 It has previously been shown that stimulation of Jurkat cells with antibodies to CD3, components of the TCR, elicits a rapid and transient phosphorylation of phospholipase C (PLC)-gamma 1, the predominant PLC isozyme in Jurkat cells, at multiple tyrosine residues and that such tyrosine phosphorylation leads to activation of PLC-gamma 1. Tyrosine 246-254 phospholipase C gamma 1 Homo sapiens 158-187 1370476-10 1992 Thus, phosphorylation of PLC-gamma 1 by PKC or PKA at serine 1248 may modulate the interaction of PLC-gamma 1 with the protein tyrosine kinase or the protein tyrosine phosphatase; this altered interaction may, at least in part, be responsible for the decreased tyrosine phosphorylation of PLC-gamma 1 seen in PMA- and forskolin-treated Jurkat cells. Tyrosine 127-135 phospholipase C gamma 1 Homo sapiens 25-36 1370476-2 1992 It has previously been shown that stimulation of Jurkat cells with antibodies to CD3, components of the TCR, elicits a rapid and transient phosphorylation of phospholipase C (PLC)-gamma 1, the predominant PLC isozyme in Jurkat cells, at multiple tyrosine residues and that such tyrosine phosphorylation leads to activation of PLC-gamma 1. Tyrosine 278-286 phospholipase C gamma 1 Homo sapiens 158-187 1370476-10 1992 Thus, phosphorylation of PLC-gamma 1 by PKC or PKA at serine 1248 may modulate the interaction of PLC-gamma 1 with the protein tyrosine kinase or the protein tyrosine phosphatase; this altered interaction may, at least in part, be responsible for the decreased tyrosine phosphorylation of PLC-gamma 1 seen in PMA- and forskolin-treated Jurkat cells. Tyrosine 127-135 phospholipase C gamma 1 Homo sapiens 98-109 1370476-3 1992 Prior incubation of Jurkat cells with PMA or forskolin, which increases intracellular cAMP concentrations, prevented tyrosine phosphorylation of PLC-gamma 1 as well as the hydrolysis of PtdIns 4,5-P2 induced by ligation of CD3. Tyrosine 117-125 phospholipase C gamma 1 Homo sapiens 145-156 1370476-4 1992 Dose-response curves of PMA and of forskolin for the inhibition of PLC-gamma 1 tyrosine phosphorylation and of PtdIns 4,5-P2 hydrolysis were similar. Tyrosine 79-87 phospholipase C gamma 1 Homo sapiens 67-78 1370476-10 1992 Thus, phosphorylation of PLC-gamma 1 by PKC or PKA at serine 1248 may modulate the interaction of PLC-gamma 1 with the protein tyrosine kinase or the protein tyrosine phosphatase; this altered interaction may, at least in part, be responsible for the decreased tyrosine phosphorylation of PLC-gamma 1 seen in PMA- and forskolin-treated Jurkat cells. Tyrosine 127-135 phospholipase C gamma 1 Homo sapiens 98-109 1730638-4 1992 Additional tyrosine-phosphorylated proteins were also found to co-immunoprecipitate with phospholipase C gamma 1 (PLC gamma 1) following EGF treatment of cells expressing 973-EGFR relative to cells expressing WT-EGFR. Tyrosine 11-19 phospholipase C gamma 1 Homo sapiens 89-112 1730638-4 1992 Additional tyrosine-phosphorylated proteins were also found to co-immunoprecipitate with phospholipase C gamma 1 (PLC gamma 1) following EGF treatment of cells expressing 973-EGFR relative to cells expressing WT-EGFR. Tyrosine 11-19 phospholipase C gamma 1 Homo sapiens 114-125 1730638-5 1992 EGF-stimulated tyrosine phosphorylation of PLC gamma 1 was found in cells expressing WT-EGFR, but not in cells expressing 973-EGFR. Tyrosine 15-23 phospholipase C gamma 1 Homo sapiens 43-54 1395933-4 1992 PLC-gamma 1 contains three tyrosine phosphorylation sites, which have been identified as residues 771, 783 and 1254. Tyrosine 27-35 phospholipase C gamma 1 Homo sapiens 0-11 1336638-0 1992 CD28 receptor crosslinking induces tyrosine phosphorylation of PLC gamma 1. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 63-74 1395933-5 1992 Phosphorylation of tyrosine residues is sufficient to increase the catalytic activity of PLC-gamma 1, though other proteins may modulate this activation. Tyrosine 19-27 phospholipase C gamma 1 Homo sapiens 89-100 1395933-7 1992 In vitro studies of PLC-gamma 1, recovered from growth factor-treated cells, indicate that activation by tyrosine phosphorylation is not due to increased sensitivity to Ca2+, a required co-factor, but is reflected in altered kinetic constants, i.e. V(max) and, to a lesser extent, Km. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 20-31 1370531-1 1992 Recently, we and others have reported tyrosine phosphorylation of phospholipase C-gamma 1 (PLC gamma 1) enzyme after CD3 activation of T cells, and have proposed that PLC gamma 1 mediates signal transduction through the T cell receptor (TCR/CD3). Tyrosine 38-46 phospholipase C gamma 1 Homo sapiens 91-102 1370531-1 1992 Recently, we and others have reported tyrosine phosphorylation of phospholipase C-gamma 1 (PLC gamma 1) enzyme after CD3 activation of T cells, and have proposed that PLC gamma 1 mediates signal transduction through the T cell receptor (TCR/CD3). Tyrosine 38-46 phospholipase C gamma 1 Homo sapiens 167-178 1683701-1 1991 Phospholipase C-gamma 1 (PLC-gamma 1) is a substrate for several receptor tyrosine kinases and its catalytic activity is increased by tyrosine phosphorylation. Tyrosine 74-82 phospholipase C gamma 1 Homo sapiens 0-23 1370350-0 1992 Sulfhydryl oxidation down-regulates T-cell signaling and inhibits tyrosine phosphorylation of phospholipase C gamma 1. Tyrosine 66-74 phospholipase C gamma 1 Homo sapiens 94-117 1370350-3 1992 Here we show that N-ethylmaleimide suppresses both CD3- and CD4-induced Ca2+ responses in human T cells correlating with a reduction in the level of phospholipase C gamma 1 (PLC gamma 1) tyrosine phosphorylation. Tyrosine 187-195 phospholipase C gamma 1 Homo sapiens 149-172 1370350-3 1992 Here we show that N-ethylmaleimide suppresses both CD3- and CD4-induced Ca2+ responses in human T cells correlating with a reduction in the level of phospholipase C gamma 1 (PLC gamma 1) tyrosine phosphorylation. Tyrosine 187-195 phospholipase C gamma 1 Homo sapiens 174-185 1370350-4 1992 The inhibition of tyrosine phosphorylation of PLC gamma 1 and additional protein substrates was observed at concentrations of N-ethylmaleimide above 20 microM, whereas lower concentrations of oxidant appeared to increase tyrosine kinase activity following cell stimulation. Tyrosine 18-26 phospholipase C gamma 1 Homo sapiens 46-57 1370350-9 1992 These data indicate that signal transduction in T cells involves the activation of PLC gamma 1 by tyrosine phosphorylation through an oxidation-sensitive intermediate between surface receptors and tyrosine kinases, perhaps including the interaction between CD4 and pp56lck. Tyrosine 98-106 phospholipase C gamma 1 Homo sapiens 83-94 1683701-1 1991 Phospholipase C-gamma 1 (PLC-gamma 1) is a substrate for several receptor tyrosine kinases and its catalytic activity is increased by tyrosine phosphorylation. Tyrosine 74-82 phospholipase C gamma 1 Homo sapiens 25-36 1683701-6 1991 All carcinomas in which tyrosine phosphorylated PLC-gamma 1 was present also expressed detectable levels of the epidermal growth factor receptor or erbB-2, two tyrosine kinases known to phosphorylate this enzyme. Tyrosine 24-32 phospholipase C gamma 1 Homo sapiens 48-59 1717999-1 1991 Stimulation of the T-cell antigen receptor (TCR) leads to tyrosine phosphorylation of a number of cellular proteins, including phospholipase C (PLC) gamma 1 and the TCR zeta chain. Tyrosine 58-66 phospholipase C gamma 1 Homo sapiens 127-156 1947181-0 1991 [The tyrosine phosphorylation and activation of PLC-gamma 1]. Tyrosine 5-13 phospholipase C gamma 1 Homo sapiens 48-59 1832154-5 1991 CD3 stimulation of T cells induces tyrosine phosphorylation of PLC gamma 1 and causes 8-10-fold higher yield of PLC activity with anti-phosphotyrosine antibody (APTyr Ab) from activated cells than from non-activated cells. Tyrosine 35-43 phospholipase C gamma 1 Homo sapiens 63-74 1832154-7 1991 Furthermore, phorbol ester and forskolin treatment of cells before CD3 stimulation reduces the level of tyrosine phosphorylation of PLC gamma 1 and the PLC activity associated with APTyr Ab. Tyrosine 104-112 phospholipase C gamma 1 Homo sapiens 132-143 1832154-8 1991 These results suggest that CD3 stimulation activates PIP2 hydrolysis by inducing tyrosine phosphorylation of PLC gamma 1, which is regulated negatively by PKC and PKA. Tyrosine 81-89 phospholipase C gamma 1 Homo sapiens 109-120 1839225-3 1991 Recent studies suggest that the TCR-activated PTK regulates PLC activation by the phosphorylation of tyrosine residues of PLC gamma 1. Tyrosine 101-109 phospholipase C gamma 1 Homo sapiens 122-133 1712101-7 1991 Thus, the TCR functions like PTK growth factor receptors, but through an indirect interaction, to induce tyrosine phosphorylation of PLC-gamma 1. Tyrosine 105-113 phospholipase C gamma 1 Homo sapiens 133-144 2061301-8 1991 These results strongly suggest that the TCR complex expressed by Jurkat cells is functionally coupled to the phosphoinositide-dependent signaling pathway through the tyrosine phosphorylation of PLC-gamma 1. Tyrosine 166-174 phospholipase C gamma 1 Homo sapiens 194-205 2061301-0 1991 T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1. Tyrosine 41-49 phospholipase C gamma 1 Homo sapiens 69-92 2061301-3 1991 In the present study, we demonstrate that antibody-mediated TCR cross-linkage results in the tyrosine phosphorylation of PLC-gamma 1. Tyrosine 93-101 phospholipase C gamma 1 Homo sapiens 121-132 2061301-7 1991 Immunoblot analyses demonstrated that TCR ligation dramatically increased the level of tyrosine-phosphorylated PLC-gamma 1 present in anti-Tyr(P) antibody immunoprecipitates from stimulated Jurkat cells. Tyrosine 87-95 phospholipase C gamma 1 Homo sapiens 111-122 2061301-7 1991 Immunoblot analyses demonstrated that TCR ligation dramatically increased the level of tyrosine-phosphorylated PLC-gamma 1 present in anti-Tyr(P) antibody immunoprecipitates from stimulated Jurkat cells. Tyrosine 139-142 phospholipase C gamma 1 Homo sapiens 111-122 1712101-0 1991 Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1. Tyrosine 61-69 phospholipase C gamma 1 Homo sapiens 89-112 1712101-8 1991 Since other studies have implicated two members of the src family of PTKs in TCR-mediated signal transduction, our findings suggest that the induction of tyrosine phosphorylation of PLC-gamma 1 by a mechanism involving a src-like kinase may be the means by which the TCR regulates PLC activity in T cells. Tyrosine 154-162 phospholipase C gamma 1 Homo sapiens 182-193 1712101-4 1991 Western blot analysis reveals that PLC-gamma 1 is tyrosine-phosphorylated in response to TCR stimulation. Tyrosine 50-58 phospholipase C gamma 1 Homo sapiens 35-46 1828897-0 1991 CD3 stimulation causes phosphorylation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line. Tyrosine 80-88 phospholipase C gamma 1 Homo sapiens 42-65 1828897-3 1991 The phosphorylation of PLC-gamma 1 occurred rapidly and transiently on both serine and tyrosine residues; tyrosine phosphorylation reached a maximum level less than 1 min after stimulation and decreased rapidly, both in the presence and in the absence of orthovanadate. Tyrosine 87-95 phospholipase C gamma 1 Homo sapiens 23-34 1828897-3 1991 The phosphorylation of PLC-gamma 1 occurred rapidly and transiently on both serine and tyrosine residues; tyrosine phosphorylation reached a maximum level less than 1 min after stimulation and decreased rapidly, both in the presence and in the absence of orthovanadate. Tyrosine 106-114 phospholipase C gamma 1 Homo sapiens 23-34 1828897-4 1991 Two-dimensional phosphopeptide map analysis revealed that the major sites of tyrosine and serine phosphorylation in PLC-gamma 1 from activated Jurkat cells are the same as those in PLC-gamma 1 from cells treated with peptide growth factors such as epidermal growth factor and platelet-derived growth factor. Tyrosine 77-85 phospholipase C gamma 1 Homo sapiens 116-127 1828897-6 1991 Thus, the current data suggest that inositol phospholipid hydrolysis triggered by the T-cell antigen receptor-CD3 complex is due, at least in part, to activation of PLC-gamma 1 and that the mechanism by which this activation is achieved involves phosphorylation of multiple tyrosine residues on PLC-gamma 1 by a nonreceptor tyrosine kinase coupled to the T-cell antigen receptor-CD3 complex. Tyrosine 274-282 phospholipase C gamma 1 Homo sapiens 165-176 2022651-4 1991 The simultaneous mutation of three major autophosphorylation sites (Y1173, Y1148, Y1068), however, caused more than a 50% decrease in EGF-induced tyrosine phosphorylation of PLC gamma 1. Tyrosine 146-154 phospholipase C gamma 1 Homo sapiens 174-185 1653029-8 1991 PDGF-induced tyrosine phosphorylation of two cellular proteins, phospholipase C gamma 1 (PLC gamma 1) and the GTPase activating protein of Ras (GAP), was assayed in epithelial cells expressing each of the mutant receptors. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 64-87 1653029-8 1991 PDGF-induced tyrosine phosphorylation of two cellular proteins, phospholipase C gamma 1 (PLC gamma 1) and the GTPase activating protein of Ras (GAP), was assayed in epithelial cells expressing each of the mutant receptors. Tyrosine 13-21 phospholipase C gamma 1 Homo sapiens 89-100 1653029-9 1991 Tyrosine phosphorylation of GAP and PLC gamma 1 was reduced markedly by the F857 mutation but not significantly by the F751 mutation. Tyrosine 0-8 phospholipase C gamma 1 Homo sapiens 36-47 2011584-8 1991 Activation of PLC in B cells by mIgM requires PTK function and is associated with tyrosine phosphorylation of PLC-gamma 1, suggesting a mechanism of PLC activation similar to that described for certain receptor PTKs. Tyrosine 82-90 phospholipase C gamma 1 Homo sapiens 110-121 35124007-4 2022 In the current study, we define how PLC-gamma1 recruitment to liposomes, which serve as a plasma membrane surrogate, and PLC-gamma1 activation are regulated both independently and additively by recruitment of PLC-gamma1 to phosphorylated LAT, by formation of the LAT-Gads-SLP-76-PLC-gamma1 tetramer, and by tyrosine phosphorylation of PLC-gamma1. Tyrosine 307-315 phospholipase C gamma 1 Homo sapiens 36-46 35124007-4 2022 In the current study, we define how PLC-gamma1 recruitment to liposomes, which serve as a plasma membrane surrogate, and PLC-gamma1 activation are regulated both independently and additively by recruitment of PLC-gamma1 to phosphorylated LAT, by formation of the LAT-Gads-SLP-76-PLC-gamma1 tetramer, and by tyrosine phosphorylation of PLC-gamma1. Tyrosine 307-315 phospholipase C gamma 1 Homo sapiens 209-219 1707501-5 1991 This involves association with, and tyrosine phosphorylation by, the ligand-bound epidermal growth factor and platelet-derived growth factor receptors, probably by means of the PLC-gamma 1-specific src homology (SH2) domain. Tyrosine 36-44 phospholipase C gamma 1 Homo sapiens 177-188 1707501-6 1991 Because EGF receptor-mediated tyrosine phosphorylation of PLC-gamma 1 stimulates catalytic activity in vitro and G proteins have been implicated in the activation of PLC, we investigated which PLC isozymes are subject to G protein regulation. Tyrosine 30-38 phospholipase C gamma 1 Homo sapiens 58-69