IndraLab
Statements
sparser
"We show that in highly motile GIV-wt cells with an intact GEF motif, EGFR autophosphorylation at Y992, Y1045, and Y1068 and the corresponding adaptor recruitment (PLCγ, cCbl, and Grb2) are enhanced, whereas in rapidly proliferating, GEF-deficient GIV-FA cells these events are suppressed."
sparser
"In pancreatic adenocarcinomas, Fibulin-3 binds EGFR (competitive to EGF) causing autophosphorylation of EGFR at Tyr-992 and Tyr-1068 and the subsequent phosphorylation of AKT at Thr-308 and ERK at Thr-202 and Tyr-204 and, thus, accelerates pancreatic adenocarcinoma growth xref ."
rlimsp
"EGFR has an extracellular ligand-binding domain, a membrane-spanning domain and a cytoplasmatic protein tyrosine kinase domain with a carboxyl terminal that contains tyrosine residues that undergo autophosphorylation during receptor activation [31-34]. Three major tyrosine sites, Y1068, Y1173 and Y1148 and two minor tyrosine sites, Y992 and Y1086, serve as sites of autophosphorylation following ligand binding or transphosphorylation by other stimuli (figure 2)."
rlimsp
"Substantial inhibition (about 90%) of rasGAP tyrosine phosphorylation by the EGF receptor occurred only when the remaining autophosphorylation site (Tyr-992) was mutated, in the context of this truncated receptor or in the full-length receptor mutated at all four other autophosphorylation sites."
rlimsp
"We show that in highly motile GIV-wt cells with an intact GEF motif, EGFR autophosphorylation at Y992, Y1045, and Y1068 and the corresponding adaptor recruitment (PLCγ, cCbl, and Grb2) are enhanced, whereas in rapidly proliferating, GEF-deficient GIV-FA cells these events are suppressed."
rlimsp
"Serum starved GIV-wt, GIV-FA, and control HeLa cells were stimulated with EGF, and EGFR autophosphorylation was assessed at Y992, Y1045, and Y1068, (docking sites of the SH2 adaptors, PLCγ1, cCbl, and Grb2) and at Y845 (the substrate for c-Src kinase that triggers mitosis; Tice ), using site-specific phospho-Tyr antibodies (Figure 2A)."
rlimsp
"In addition, the conversion of Tyr992, which is an EGFr ligand-induced autophosphorylation site, to phenylalanine also increases the rate of receptor internalization. However, the mutation of Tyr992 to a glutamate residue does not alter the receptor internalization rate. In addition, the truncation of the EGFr at glutamate 996 reduces the internalization rate by half. This result confirms previous reports that residues immediately C-terminal to Glu996 are necessary to allow the normal rate of ligand-induced receptor endocytosis. The data suggest that negative charge in the vicinity of Tyr992, and potentially the phosphorylation of the EGFr at Tyr992, reduces the rate of ligand-induced receptor endocytosis."
rlimsp
"Requirement of autophosphorylated tyrosine 992 of EGF receptor and its docking protein phospholipase C gamma 1 for membrane ruffle formation. Stimulation of the epidermal growth factor receptor (EGFR) produces membrane ruffles through the small G protein Rac1; however, the signaling pathway from EGFR to Rac1 has not yet been clarified. Here, we show that autophosphorylation of EGFR at tyrosine 992 is required for EGF-induced membrane ruffle formation in CHO cells. Signaling from the autophosphorylated tyrosine 992 appears to be mediated by phospholipase C (PLC) gamma 1."