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- W2010767308 abstract "c-Src is a membrane-associated tyrosine kinase that can be activated by many types of extracellular signals, and can regulate the function of a variety of cellular protein substrates. We demonstrate that epidermal growth factor (EGF) and beta-adrenergic receptors activate c-Src by different mechanisms leading to the phosphorylation of distinct sets of c-Src substrates. In particular, we found that EGF receptors, but not beta(2)-adrenergic receptors, activated c-Src by a Ral-GTPase-dependent mechanism. Also, c-Src activated by EGF treatment or expression of constitutively activated Ral-GTPase led to tyrosine phosphorylation of Stat3 and cortactin, but not Shc or subsequent Erk activation. In contrast, c-Src activated by isoproterenol led to tyrosine phosphorylation of Shc and subsequent Erk activation, but not tyrosine phosphorylation of cortactin or Stat3. These results identify a role for Ral-GTPases in the activation of c-Src by EGF receptors and the coupling of EGF to transcription through Stat3 and the actin cytoskeleton through cortactin. They also show that c-Src kinase activity can be used differently by individual extracellular stimuli, possibly contributing to their ability to generate unique cellular responses." @default.
- W2010767308 created "2016-06-24" @default.
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- W2010767308 date "2000-02-15" @default.
- W2010767308 modified "2023-09-27" @default.
- W2010767308 title "An EGF receptor/Ral-GTPase signaling cascade regulates c-Src activity and substrate specificity" @default.
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- W2010767308 doi "https://doi.org/10.1093/emboj/19.4.623" @default.
- W2010767308 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/305600" @default.
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