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EGFR phosphorylates STAT3 on Y705. 21 / 24
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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."
20030624
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"As a key transcription factor for cell survival and proliferation, STAT3 can be phosphorylated in Tyr-705 and subsequently activated by various receptor tyrosine kinases (EGFR, FGFR, and IGF-1R, etc.), receptor-associated kinases such as JAK, and non-receptor kinases such as Src and Abl."
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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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"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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"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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"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."
35932642
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"We discovered that EGFR T790M-cis-L792F mutation activated phosphorylation of STAT3 Tyr705 and thus promoted its specific binding to IL4 promoter, which induced resistance to osimertinib."
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"EGFR T790M-cis-L792F mutation promoted IL-4 expression and secretion by activating STAT3 Tyr705 phosphorylation and its specific binding to IL4 promoter."
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"As the central switch macrophages from the pro-inflammatory to the anti-inflammatory subtype, IL-4 highlights the M2 polarization of TAM, as previously reported.38 39 This evidence demonstrates that EGFR T790M-cis-L792F cell-induced osimertinib resistance promotes macrophage M2 polarization through IL-4 activity.As a transcription factor, STAT3 is phosphorylated by downstream pathways when EGFR is activated.40 Therefore, we also confirmed that EGFR T790M-cis-L792F mutation activating STAT3 phosphorylation at the Tyr705 site (not at Ser727) induced IL-4 transcription."
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"In line with these findings, Igfbp2-deficiency resulted in a significant increase in the EGFR-STAT3 pathway, leading to enhanced expression of the gene network associated with lipogenesis and steatosis in hepatocytes.Previous studies showed that EGFR can directly interact with and phosphorylate STAT3 at Tyr-705 and thereby activates it for DNA binding upon EGF stimulation [48]."
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"The activation of STAT3-dependent genes starts with tyrosine705 phosphorylation of STAT3 by EGFR. xref suggested that the rapid tyrosine phosphorylation followed by the STAT3-DNA complex formation is unaffected by the EGFR inhibition in HNSCC cell lines."
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"Polysaccharide peptide therapy reduced intracellular EGFR signaling cascade intermediates, such as EGFR, p-EGFR (Tyr1068), STAT3, p-STAT3 (Tyr705), and c-Jun expression and phosphorylation (Figure 3)."
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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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"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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"EGFR, phosphorylated (p)-EGFR (Y845, Y1068, Y1086, and Y1197), Akt, p-Akt (serine [S473]), 4E-BP1, p-4E-BP1 (threonine [T]37/46), STAT3, and p-STAT3 (Y705) were selected based on the RayBio Human EGFR Phosphorylation Antibody Array 1 results."
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"We had previously shown that saracatinib, a dual EGFR/SRC inhibitor that blocks Y705 and S727 phosphorylation of STAT3, reverses Ispinesib resistance."
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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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"Previous study reported that JAK, ERK, EGFR kinase and Src could phosphorylate STAT3 on Y705 and activate STAT3 [40–43]."
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"In this study, we found that inhibition of EGFR using either genetic or pharmacologic strategies attenuates STAT3 Tyr705 phosphorylation and activation in Tsc1- or Tsc2-deficient cells, while overexpression of EGFR facilitates the phosphorylation and activation of STAT3 (Figure 7)."
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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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