IndraLab
Statements
rlimsp
"Here, we used a NIH 3T3 cell transformation system to underscore the critical involvement of signaling through Src, orchestrated by the Src phosphorylation site on EGFR (Y845), which appears crucial in linking mutant EGFRs to oncogenesis and constitutive activation of specific signaling pathways."
sparser
"The protein tyrosine kinase c-Src can directly phosphorylate Tyr residues in the kinase domain HER2 [ xref , xref ] and the cytoplasmic tail of EGFR [ xref ], allowing the formation of stable homo- or heterocomplexes with other receptors or the binding of scaffold proteins and the activation of signal transduction."
reach
"Activated Src leads to phosphorylation of epidermal growth factor receptor (EGFR) and other receptor tyrosine kinases (RTK) that, in turn, activate diverse downstream intermediates of the signaling cascade, including phospholipase C (PLC-γ), G-protein Ras and mitogen-activated protein kinases (MAPK) [12] (Figure 7)."
sparser
"The EGFR can be transactivated either by enhanced “inside-out signaling” that would increase cell surface shedding of EGFR ligands such as pro HB-EGF by stimulating metalloproteinases of the ADAM (a disintegrin and metalloproteinase) family ( xref ; xref ; xref ) or by intracellular activation of non-receptor tyrosine kinase c-Src ( xref ), which phosphorylates the EGFR on tyrosine residue 845 and 1101 and results in receptor activation ( xref )."
rlimsp
"It is well known that Src can phosphorylate EGFR on Y845, but it has been reported that Src phosphorylation on this residue does not affect EGFR autokinase activity [13], suggesting that EGFR Y1173 phosphorylation should not be decreased by Src inhibition, unless the anti-Src agents have cross-reactivity with EGFR."
reach
"It is well known that Src can phosphorylate EGFR on Y845, but it has been reported that Src phosphorylation on this residue does not affect EGFR autokinase activity [XREF_BIBR], suggesting that EGFR Y1173 phosphorylation should not be decreased by Src inhibition, unless the anti-Src agents have cross-reactivity with EGFR."
"When co-overexpressed, the epidermal growth factor receptor (EGFR) and c-Src cooperate to cause synergistic increases in EGF-induced DNA synthesis, soft agar colony growth, and tumor formation in nude mice. This synergy is dependent upon c-Src-mediated phosphorylation of a unique tyrosine on the EGFR, namely, tyrosine 845 (Y845). "
"In this study, we demonstrated that c-Src-dependent phosphorylation of tyrosine 845 (Tyr 845) on EGFR was required for DNA synthesis induced by the G protein-coupled agonists, endothelin (ET) and lysophosphatidic acid (LPA), and the cytokine, growth hormone (GH), in murine fibroblast and breast cancer model systems. "
"Revealed that peptides derived from egfr residues y992, y1086, y1101, and y1148 bound directly to the sh2 domain of c-src (figure 8c). These experiments demonstrate that a specific subset of egfr receptor c-src phosphorylation sites are also ligands for the sh2 domain of c-src.Cellular src functions as a co-transducer of transmembrane signals emanating from a variety of growth factor receptors, including egfr"
"A subset of peptides corresponding to the eight possible tyrosine phosphorylation sites within the EGFR autophosphorylation domain was demonstrated to bind to the SH2 domain of c-src. Those which bound to the SH2 domain included peptides derived from EGFR sequences flanking Y992, Y1086, Y1101, and Y1148. These data indicate that specific EGF receptor c-src phosphorylation sites are also ligands for the SH2 domain of c-src. "