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|標題:||Src phosphorylates Grb2-associated binder 1 upon hepatocyte growth factor stimulation||作者:||Chan, P.C.
|關鍵字:||receptor tyrosine kinase;focal adhesion kinase;epithelial;morphogenesis downstream;signal-regulated kinase;docking protein gab1;grb2 binding-site;c-met;adapter protein;factor hgf;phosphatidylinositol 3-kinase||Project:||Journal of Biological Chemistry||期刊/報告no：:||Journal of Biological Chemistry, Volume 278, Issue 45, Page(s) 44075-44082.||摘要:||
Grb2-associated binder 1 (Gab1) is known to play an important role in hepatocyte growth factor (HGF) signaling, which rapidly becomes tyrosine-phosphorylated upon HGF stimulation. In this study, we found that the tyrosine phosphorylation of Gab1 in the cells derived from Src/Yes/Fyn null mouse embryos was similar to40% lower than that in their wild type counterparts upon HGF stimulation. Increased expression of wild-type Src enhanced HGF-induced phosphorylation of Gab1, and, in contrast, expression of the Src kinase-deficient mutant or treatment of the specific Src inhibitor PP1 suppressed it. Expression of a constitutively active Src mutant (Y527F) or oncogenic v-Src led to a prominent increase in Gab1 phosphorylation independent of HGF stimulation. Moreover, Src interacted with Gab1 via both its Src homology 2 and 3 domains and was capable of phosphorylating purified Gab1 in vitro. Finally, the increased phosphorylation of Gab1 by Src selectively potentiated HGF-induced activation of ERK and AKT. Taken together, our results establish a new role for Src in HGF-induced Gab1 phosphorylation.
|Appears in Collections:||生命科學院|
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