IndraLab

Statements

EGF leads to the phosphorylation of EGFR on Y1110. 8 / 10
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"This downregulation of EGFR was accompanied by a pronounced and significant increase in the activating EGFR phosphorylation at Tyr1086 in response to EGF."
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"EGF stimulation resulted in rapid phosphorylation of EGFR (pEGFR Y1110) which was almost completely blocked by the EGFR kinase inhibitor, tyrphostin (AG1478) (XREF_FIG)."
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"Specifically, it was found that EGF-induced EGFR phosphorylation of Y845, Y1086, and Y1173 returned to baseline much faster, as compared to phosphorylation in response to epigen and epiregulin ( xref )."
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"Importantly, lenvatinib also significantly downregulated EGFR phosphorylation at the Tyr1086 site induced by EGF (Fig. 2F)."
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"As expected, EGF incubation greatly increased phosphorylation of EGFR (Tyr 1068, Tyr 1086, Tyr 845) and extracellular signal-regulated kinase (ERK), but not JAK, Src or STATs."
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"EGF stimulation increased EGFR phosphorylation on Tyr1173 and Tyr1086 (XREF_FIG and XREF_SUPPLEMENTARY)."
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"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."
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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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