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EGF — STAT5B

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: STAT5B → EGF (increases, EGF Activity) Kloth et al., J Biol Chem 2003*
  Evidence: This activation is completely ablated when the kinase-defective EGFR (K721A) or the tyrosine mutant of the EGFR (Y845F) are transfected, thus demonstrating that both the kinase activity and tyrosine 845 are required for EGF-induced transcriptional activation of STAT5b.
• OpenBEL Selventa BEL large corpus: STAT5B → EGF (increases) Kloth et al., J Biol Chem 2003*
  Evidence: use of site-specific tyrosine mutants demonstrates that EGF-induced phosphorylation of STAT5b involves not only tyrosine 699 of STAT5b, which is required for its transcriptional activation, but also three previously identified tyrosines in the C terminus of STAT5b (Tyr(725)/Tyr(740)/Tyr(743))

Text-mined interactions from Literome

Guren et al., Biochem Biophys Res Commun 1999 : EGF induced activation of Stat1, Stat3, and Stat5b is unrelated to the stimulation of DNA synthesis in cultured hepatocytes ... In freshly isolated hepatocytes, EGF activated Stat1, Stat3, and, particularly, Stat5b ... In these cells EGF did not detectably activate Stat1, Stat3, or Stat5b but markedly stimulated MAP kinase ( Erk1/2 )
Kloth et al., J Biol Chem 2002 : Novel activation of STAT5b in response to epidermal growth factor ... The data presented here demonstrate that, in contrast to activation by the cytokine, growth hormone (GH), the activation of STAT5b by the growth factor, epidermal growth factor (EGF), requires overexpression of the EGF receptor (EGFR) ... We have shown that EGF activates STAT5b not only in a HEK293 cell model in which the EGFR is stably overexpressed but also in the MDA-MB468 breast cancer cell line ... Because overexpression of the EGFR is common in many cancers, including advanced breast cancer, characterization of EGF induced STAT5b may have direct implications in therapeutic applications
Kloth et al., J Biol Chem 2003 : We demonstrate that 1 ) activation of STAT5b by EGF requires overexpression of the EGFR, 2 ) co-overexpression of c-Src alone does not result in EGF induced activation of STAT5b but enhances that seen in EGFR overexpressing cells, and 3 ) EGF induced tyrosine phosphorylation of STAT5b requires Tyr ( 845 ) of the EGFR ... Furthermore, the stable overexpression of a kinase-defective c-Src in the context of EGFR overexpression results in a decrease in the tyrosine phosphorylation of STAT5b in response to EGF and a more dramatic decrease in EGF induced transcriptional activation of STAT5b , suggesting an integral role for c-Src in the physiological actions of STAT5b ... Finally, the use of site-specific tyrosine mutants demonstrates that EGF induced phosphorylation of STAT5b involves not only tyrosine 699 of STAT5b, which is required for its transcriptional activation, but also three previously identified tyrosines in the C terminus of STAT5b ( Tyr ( 725 ) /Tyr ( 740 ) /Tyr ( 743 ) )
Guren et al., J Cell Physiol 2003 : EGF receptor mediated , c-Src dependent, activation of Stat5b is downregulated in mitogenically responsive hepatocytes ... We previously showed that Stat5b was activated by EGF in rat hepatocytes in primary monolayer culture ... In the present study, we found that EGF induced tyrosine phosphorylation of Stat5b both on Tyr-699, which correlated with specific DNA binding activity, and also on other tyrosine residues ... The Src tyrosine kinase inhibitor CGP77675 blocked the EGF induced activation of Stat5b , but did not affect the Stat5b activation by growth hormone (GH) or prolactin (PRL) ... The Stat5b response to EGF was most pronounced soon ( 3 h ) after plating ( early G ( 1 ) ) and at high cell density ( 50,000 hepatocytes per cm ( 2 ) ) ... In hepatocytes at 24 h of culturing ( mid/late G ( 1 ) ) with 20,000 cells per cm ( 2 ), EGF induced strong phosphorylation of the EGF receptor, as well as Shc and ERK, and stimulated DNA synthesis, but did not activate Stat5b , although the Stat5b response to GH or PRL was retained ... The results show that EGF induces tyrosine phosphorylation and DNA binding activity of Stat5b in a manner different from GH and PRL, apparently by a Src dependent mechanism
Boerner et al., Mol Endocrinol 2005 (Breast Neoplasms) : Introduction of ERalpha and treatment with E2 decreased EGF induced tyrosine phosphorylation of STAT5b , basal and EGF induced STAT5 mediated transcription, and EGF stimulated DNA synthesis in these cells