IndraLab

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EGF leads to the phosphorylation of EGFR on Y1016. 27 / 27
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"Although both AR and EGF stimulate EGFR phosphorylation at Tyr992, we and others have observed that EGF stimulates greater EGFR phosphorylation at Tyr992 than does AR."
22260327
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"PKG II Blocks EGF-induced Tyr 992 and Tyr 1068 Phosphorylation of EGFR."
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"We found that N-formyl-methionyl-leucyl-phenylalanine, an FPR agonist peptide, rapidly induced EGFR phosphorylation at tyrosine residue (Tyr) 992, but not residues 846, 1068, or 1173, in glioblastoma cells, whereas all these residues were phosphorylated after only EGF treatment."
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"PKG II inhibited EGF-induced migration activity and blocked EGF-initiated signal transduction of PLCγ1 and MAPK/ERK-mediated pathways through preventing EGF-induced Tyr 992 and Tyr 1068 phosphorylation of EGFR."
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"Both AR and EGF stimulate EGFR phosphorylation at Tyr992 (XREF_FIG), one of the major sites of EGFR phosphorylation following stimulation with AR."
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"We found that EGF treatment induced the phosphorylation of EGFR (Tyr992) and ERK1/2 (Thr202 and Tyr204) in a time dependent manner in OVCAR-5 and SKOV-3 cells."
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"We found that EGF induced similar phosphorylation of tyrosine-992 (Y992) of the epidermal growth factor receptor (pY992-EGFR) in control, Tln Ko and Kind Ko cells."
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"Both EGF and AR stimulate phosphorylation of EGFR Tyr992."
22260327
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"Interestingly, HeLa cells transfected with the siRNA for PIP5KIα displayed a marked reduction in both their basal (which was high enough in three out of four batches of cells to allow detection by WB), and EGF-induced EGFR Y992 phosphorylation ( xref )."
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"XREF_FIG presents a representative western blot showing the time-course of EGFR Tyr992 phosphorylation following EGF stimulation."
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"TABLE V Survey of cell signaling proteins that show a reaction to EGF ligand stimulation over a 180-min time course - 500ng/mL EGF results"
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"In contrast, overexpression of PTP μ decreased EGF-stimulated EGFR Y992 and Y1068 phosphorylation."
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"We found that EGF induced similar phosphorylation of tyrosine 992 (Y992) of the epidermal growth factor receptor (pY992-EGFR) in control, Tln Ko and Kind Ko cells."
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"EGF abundantly stimulated EGFR phosphorylation at Tyr992, Tyr1045, and Tyr1068, whereas amphiregulin did not stimulate phosphorylation at Tyr992 in either the NHBE or the BSMC."
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"Purified EGFR was phosphorylated in vitro with EGF in the presence of various synthetic peptides."
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"24,25 Also in our experiments, whereas EGF abundantly stimulated EGFR phosphorylation at Tyr992 in NHBEs, amphiregulin did not."
19895983
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"EGF abundantly stimulated EGFR phosphorylation at Tyr992, Tyr1045, and Tyr1068, whereas amphiregulin did not stimulate phosphorylation at Tyr992 in either the NHBE or the BSMC."
19895983
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"TSP1 and its EGF like repeats also increased phosphorylation of EGFR Tyr 845, Tyr 992, Tyr 1045, Tyr 1086, and Tyr 1173, activated phospholipase Cgamma, and increased cell migration."
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"In contrast, overexpression of PTPmu decreased EGF stimulated EGFR Y992 and Y1068 phosphorylation."
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"We note that EGF stimulates greater EGFR phosphorylation at Tyr992 than does AR."
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"It is well established that EGF stimulates the phosphorylation of five major tyrosine residues at the EGFR C-terminus, including Y992, Y1068, Y1086, Y1148 and Y1173."
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"This indicated that PKG II could prevent EGF-induced Tyrosine 992 and Tyrosine 1068 phosphorylation of EGFR and consequently inhibit PLCγ1-mediated and MAPK/ERK–mediated signaling."
23613900
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"Western blot studies indicated that EGF induces phosphorylation of EGFR-Tyr992."
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"Furthermore, reduced expression of PTPRM resulted in an increased phosphorylation of tyrosine 992 of EGFR (pY992) by EGF, a docking site for phospholipase C γ 1 (PLCγ1) to activate PLCγ1, thus leading to increased cell migration in both wounding and chemotaxis assays xref , xref ."
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"The goal of these studies was to determine whether PTP1B plays a role in regulating EGF-induced Tyr992 phosphorylation of EGFR and cell cycle entry in rat corneal endothelial cells."
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"We found that EGF treatment induced the phosphorylation of EGFR (Tyr992), AKT (Ser473), and ERK (Thr202 and Tyr204) in a time dependent manner in SKOV3 and HO8910 cells (XREF_FIG)."
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"24,25 Also in our experiments, whereas EGF abundantly stimulated EGFR phosphorylation at Tyr992 in NHBEs, amphiregulin did not."
19895983