IndraLab

Statements


EGFR phosphorylates STAT3 on Y705. 10 / 10
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"Interestingly, ablation of EGFR and c-RAF expression in NC cells induced increased phosphorylation of STAT3 at the canonical Tyr705 residue (Figure 5C)."

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"2 Phosphorylation of Stat3 at Y705 is often mediated by JAK1, epidermal growth factor receptor, or Src and is required for Stat3 homo- or hetero-dimerization, nuclear translocation, and DNA binding."

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"Phosphorylation of the STAT3 Y705 residue can be induced by cytokines (IL-6, IFN-alpha), growth factors (EGFR, EGFRvIII, HER2 and PDGFR) and non receptor tyrosine kinases (Src and all the JAK family proteins) [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"In addition, the presence of EGFR in CHO cells markedly enhanced T. gondii induced early Y705 STAT3 phosphorylation (XREF_SUPPLEMENTARY)."

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"EGFR T790M-cis-L792F mutation upregulated phosphorylation of STAT3 Tyr705 and promoted its specific binding to IL4 promoter, enhancing IL-4 expression and secretion and inducing macrophage M2 polarization."

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"This form of resistance requires dual phosphorylation of STAT3 residues Y705 and S727, mediated by SRC and epidermal growth factor receptor (EGFR), respectively."

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"With regard to signal transducer and activator of transcription 3 (STAT3), cell-surface EGFR and EGFRvIII physically associate with and phosphorylate STAT3 at Y705 and in turn, phosphorylated STAT3 dimerizes and translocates into the cell nucleus to regulate gene expression."

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"With regard to signal transducer and activator of transcription 3 (STAT3), cell-surface EGFR and EGFRvIII physically associate with and phosphorylate STAT3 at Y705 and in turn, phosphorylated STAT3 dimerizes and translocates into the cell nucleus to regulate gene expression."

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"36 A compound binding to the SH2 domain of STAT3 is therefore expected to block the binding of STAT to EGFR and subsequent phosphorylation of Y705 of STAT3."

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"Here, we found that inhibition of EGFR by erlotinib induces STAT3 phosphorylation at Tyr705 in association with increased Bcl2/Bcl-XL at both mRNA and protein levels in various human lung cancer cells."