Relationship between Phospholipase C, Tyrosine-Kinases and Cytoskeleton in Thrombin-Stimulated Platelets

1993 ◽  
pp. 39-44
Author(s):  
Christine Guinebault ◽  
Monique Plantavid ◽  
Bernard Payrastre ◽  
Pascal Grondin ◽  
Claire Racaud-Sultan ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases

Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase C-gamma in quiescent BALB/c 3T3 cells

1989 ◽  
Vol 9 (7) ◽  
pp. 2934-2943
Author(s):  
M I Wahl ◽  
N E Olashaw ◽  
S Nishibe ◽  
S G Rhee ◽  
W J Pledger ◽  
...  
Keyword(s):  
Growth Factor ◽  
Phospholipase C ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
Hormonal Regulation ◽  
Growth Factor Receptor ◽  
Fold Increase ◽  
Platelet Derived Growth Factor ◽  
3T3 Cells ◽  
Pdgf Stimulation

Platelet-derived growth factor (PDGF) stimulates the proliferation of quiescent fibroblasts through a series of events initiated by activation of tyrosine kinase activity of the PDGF receptor at the cell surface. Physiologically significant substrates for this or other growth factor receptor or oncogene tyrosine kinases have been difficult to identify. Phospholipase C (PLC), a key enzyme of the phosphoinositide pathway, is believed to be an important site for hormonal regulation of the hydrolysis of phosphatidylinositol 4,5-bisphosphate, which produces the intracellular second-messenger molecules inositol 1,4,5-trisphosphate and 1,2-diacylglycerol. Treatment of BALB/c 3T3 cells with PDGF led to a rapid (within 1 min) and significant (greater than 50-fold) increase in PLC activity, as detected in eluates of proteins from a phosphotyrosine immunoaffinity matrix. This PDGF-stimulated increase in phosphotyrosine-immunopurified PLC activity occurred for up to 12 h after addition of growth factor to quiescent cells. Interestingly, the PDGF stimulation occurred at 3 as well as 37 degrees C and in the absence or presence of extracellular Ca2+. Immunoprecipitation of cellular proteins with monoclonal antibodies specific for three distinct cytosolic PLC isozymes demonstrated the presence of a 145-kilodalton isozyme, PLC-gamma (formerly PLC-II), in BALB/c 3T3 cells. Furthermore, these immunoprecipitation studies showed that PLC-gamma is rapidly phosphorylated on tyrosine residues after PDGF stimulation. The results suggest that mitogenic signaling by PDGF is coincident with tyrosine phosphorylation of PLC-gamma.

scholarly journals Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in vivo and in vitro

Cell ◽  
1989 ◽  
Vol 57 (7) ◽  
pp. 1109-1122 ◽  
Author(s):  
Jill Meisenhelder ◽  
Pann-Ghill Suh ◽  
Sue Goo Rhee ◽  
Tony Hunter
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases ◽  
Egf Receptor ◽  
Protein Tyrosine Kinases ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinases

scholarly journals A protein that is highly related to GTPase-activating protein-associated p62 complexes with phospholipase C gamma.

1994 ◽  
Vol 14 (8) ◽  
pp. 5466-5473 ◽  
Author(s):  
M C Maa ◽  
T H Leu ◽  
B J Trandel ◽  
J H Chang ◽  
S J Parsons
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases ◽  
Egf Receptor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gtpase Activating Protein ◽  
Glutathione S Transferase ◽  
Sh2 Domains ◽  
Phospholipase C Gamma

p62 is a highly tyrosyl phosphorylated protein that was first identified in immunoprecipitates of the GTPase-activating protein (GAP) of p21ras from cells transformed by oncogenic nonreceptor tyrosine kinases or stimulated through tyrosine kinase receptors (C. Ellis, M. Moran, F. McCormick, and T. Pawson, Nature 343:377-381, 1991). In this article we describe a highly related 62-kDa protein that becomes tyrosyl phosphorylated and associated with phospholipase C gamma (PLC gamma) in C3H10T1/2 cells stimulated with epidermal growth factor (EGF) or transformed by v-src. GAP-associated and PLC gamma-associated p62 comigrated in one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and exhibited nearly identical phosphotryptic peptide patterns. That the association of p62 with PLC gamma was direct and not mediated through binding of GAP-p62 to PLC gamma or to the EGF receptor (and coprecipitation of the receptor with PLC gamma) was demonstrated by (i) the inability to detect GAP in PLC gamma immunocomplexes or PLC gamma in GAP immunocomplexes, (ii) the association of p62 with PLC gamma in v-src-transformed cells in the absence of EGF stimulation, and (iii) in vitro solution binding and direct blotting of p62 with a glutathione S-transferase fusion protein containing the Src homology 2 (SH2) domains of PLC gamma. Unlike GAP, whose N-terminal SH2 mediates the interaction between GAP and p62, PLC gamma was found to require both its N- and C-terminal SH2 regions for p62 binding. These studies demonstrate that a protein identical to or highly related to GAP-associated p62 binds PLC gamma and suggest a means by which "cross-talk" between PLC gamma- and GAP-mediated signalling may occur.

scholarly journals Tyrosine phosphorylation of Grb2-associated proteins correlates with phospholipase C gamma 1 activation in T cells.

1996 ◽  
Vol 16 (6) ◽  
pp. 2823-2829 ◽  
Author(s):  
D G Motto ◽  
M A Musci ◽  
S E Ross ◽  
G A Koretzky
Keyword(s):  
T Cell ◽  
Phospholipase C ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
Inositol Phosphate ◽  
Critical Role ◽  
Chimeric Protein ◽  
Sh2 Domain ◽  
Mitogen Activated Protein Kinase ◽  
Phospholipase C Gamma

Ligation of the T-cell antigen receptor (TCR) results in the rapid activation of several protein tyrosine kinases, with the subsequent phosphorylation of numerous cellular proteins. We investigated the requirement for tyrosine phosphorylation of proteins which bind the Grb2 SH2 domain in TCR-mediated signal transduction by transfecting the Jurkat T-cell line with a cDNA encoding a chimeric protein designed to dephosphorylate these molecules. Stimulation of the TCR on cells expressing this engineered enzyme fails to result in sustained tyrosine phosphorylation of a 36-kDa protein likely to be the recently cloned pp36/Lnk. 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. TCR-mediated Ras and mitogen-activated protein kinase activation remain intact in cells expressing the engineered phosphatase. 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.

scholarly journals Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1.

1995 ◽  
Vol 15 (1) ◽  
pp. 186-197 ◽  
Author(s):  
S Richard ◽  
D Yu ◽  
K J Blumer ◽  
D Hausladen ◽  
M W Olszowy ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Tyrosine Phosphorylation ◽  
Tyrosine Kinases ◽  
Sh3 Domain ◽  
Sh2 Domain ◽  
Src Family Kinases ◽  
Src Family Kinase ◽  
Sh3 Domains ◽  
Sh2 Domains ◽  
Src Family Tyrosine Kinases

src family tyrosine kinases contain two noncatalytic domains termed src homology 3 (SH3) and SH2 domains. Although several other signal transduction molecules also contain tandemly occurring SH3 and SH2 domains, the function of these closely spaced domains is not well understood. To identify the role of the SH3 domains of src family tyrosine kinases, we sought to identify proteins that interacted with this domain. By using the yeast two-hybrid system, we identified p62, a tyrosine-phosphorylated protein that associates with p21ras GTPase-activating protein, as a src family kinase SH3-domain-binding protein. Reconstitution of complexes containing p62 and the src family kinase p59fyn in HeLa cells demonstrated that complex formation resulted in tyrosine phosphorylation of p62 and was mediated by both the SH3 and SH2 domains of p59fyn. The phosphorylation of p62 by p59fyn required an intact SH3 domain, demonstrating that one function of the src family kinase SH3 domains is to bind and present certain substrates to the kinase. As p62 contains at least five SH3-domain-binding motifs and multiple tyrosine phosphorylation sites, p62 may interact with other signalling molecules via SH3 and SH2 domain interactions. Here we show that the SH3 and/or SH2 domains of the signalling proteins Grb2 and phospholipase C gamma-1 can interact with p62 both in vitro and in vivo. Thus, we propose that one function of the tandemly occurring SH3 and SH2 domains of src family kinases is to bind p62, a multifunctional SH3 and SH2 domain adapter protein, linking src family kinases to downstream effector and regulatory molecules.

Phospholipase C and Src Tyrosine Kinases Mediate Neurotensin-Stimulated Cl-Secretion in Rabbit Proximal Colon

2004 ◽  
Vol 49 (7/8) ◽  
pp. 1318-1326 ◽  
Author(s):  
Roli Prasad ◽  
Jayashree Venkatasubramanian ◽  
Milen Amd ◽  
Mrinalini Chatta Rao
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases ◽  
Proximal Colon ◽  
Cl Secretion ◽  
Src Tyrosine Kinases

scholarly journals G Protein-coupled Receptor-induced Sensitization of Phospholipase C Stimulation by Receptor Tyrosine Kinases

2000 ◽  
Vol 275 (42) ◽  
pp. 32603-32610 ◽  
Author(s):  
Martina Schmidt ◽  
Markus Frings ◽  
Marie-Luise Mono ◽  
Yuanjian Guo ◽  
Paschal A. Oude Weernink ◽  
...  
Keyword(s):  
Phospholipase C ◽  
G Protein ◽  
Tyrosine Kinases ◽  
Receptor Tyrosine Kinases ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

Phosphoinositide 3-kinase-dependent regulation of phospholipase Cγ

2007 ◽  
Vol 35 (2) ◽  
pp. 229-230 ◽  
Author(s):  
T. Maffucci ◽  
M. Falasca
Keyword(s):  
Phospholipase C ◽  
Tyrosine Kinases ◽  
Receptor Tyrosine Kinases ◽  
Second Messengers ◽  
Pleckstrin Homology Domain ◽  
Ph Domain ◽  
Pleckstrin Homology ◽  
Functional Roles ◽  
Phosphoinositide 3 Kinase

Activation of the enzyme PLC (phospholipase C) leads to the formation of second messengers Ins(1,4,5)P3 and diacylglycerol. RTKs (receptor tyrosine kinases) activate this reaction through PLCγ isoenzymes. It has been shown that PI3K (phosphoinositide 3-kinase) may regulate PLCγ activity through the interaction of PI3K product PtdIns(3,4,5)P3 and the PLCγ PH domain (pleckstrin homology domain). Here, we analyse the potential functional roles of the PI3K/PLC pathway.

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