Regular ArticleEGF Receptor Deletions Define a Region Specifically Mediating Stat Transcription Factor Activation
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Inhibition of STAT3 activation by KT-18618 via the disruption of the interaction between JAK3 and STAT3
2014, Biochemical PharmacologyCitation Excerpt :In contrast, the binding between STAT3 and JAK2 was not inhibited in the same condition (Fig. 4B). In previous reports, it was shown that EGFR recruits STAT molecules through tyrosine 1068 and tyrosine 1086 and leads to STAT3 phosphorylation or activation [38,39]. Another tyrosine kinase, Src kinase, has been reported to play a role in mediating constitutive STAT activation in many human cancer cell lines [40].
Epithelial to mesenchymal transition promotes breast cancer progression via a fibronectin-dependent STAT3 signaling pathway
2013, Journal of Biological ChemistryCitation Excerpt :To address this question, we engineered NR6 cells, which lack endogenous EGFR expression to stably express equivalent levels of either wild-type EGFR (WT-EGFR) or an EGFR mutant with a dialanine substitution for Leu-679 and Leu-680 (EGFR-AA) (5, 34, 35). Importantly, the EGFR-AA mutant is defective for Tyr-845 phosphorylation by SRC, an event that is necessary for STAT3 activation (36). Accordingly, EGF stimulation of WT-EGFR expressing cells elicited robust phosphorylation of EGFR at Tyr-845 and a STAT3 reaction that failed to occur in EGFR-AA expressing cells (Fig. 1A).
Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin
2009, Biochimica et Biophysica Acta - Molecular Cell ResearchSTAT5 phosphorylation in malignant melanoma is important for survival and is mediated through SRC and JAK1 kinases
2006, Journal of Investigative DermatologyMembrane-associated STAT3 and PY-STAT3 in the cytoplasm
2006, Journal of Biological ChemistryERBB4/HER4 potentiates STAT5A transcriptional activity by regulating novel STAT5A serine phosphorylation events
2005, Journal of Biological ChemistryCitation Excerpt :In the mammary gland, STAT5A regulates multiple pregnancy-induced developmental events including specification of ductal epithelium to a secretory phenotype, epithelial terminal differentiation, and activation of milk gene expression during lactation (1-5). STAT5A activity is regulated by phosphorylation events at specific residues through the actions of receptor tyrosine kinases, cytokine receptors, and non-receptor tyrosine kinases (6, 7). Phosphorylation of the regulatory Tyr-694 is indispensable for STAT5A transcriptional activity and has been used as a biochemical indicator of STAT5A transcriptional activation (8).