Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins.
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چکیده
منابع مشابه
Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins.
The products of the shc gene appear to be substrates for activated oncogenic tyrosine kinases, such as v-Src and v-Fps and activated tyrosine kinase receptors like the epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors. We investigated whether the Shc proteins are targets for the activated insulin receptor tyrosine kinase. Here we show that the 46- and 52-kDa Shc ...
متن کاملTaxol mediates serine phosphorylation of the 66-kDa Shc isoform.
In the human lung carcinoma cell line A549, Taxol (20 nM) causes a decreased electrophoretic mobility of the 66-kDa Shc isoform (p66shc), beginning 4 h after drug exposure, and reaching a maximum at 9-18 h. No shift was observed for the 52- and 46-kDa isoforms of Shc. The electrophoretic mobility shift of p66shc caused by Taxol is not the result of tyrosine phosphorylation, and there is no indi...
متن کاملThe functional significance of Shc in insulin signaling as a substrate of the insulin receptor.
Shc is composed of 46-, 52-, 66-kDa isoforms which arise from alternative splicing of the primary Shc transcript. Upon insulin stimulation, the activated insulin receptor interacts with Shc. The NPXY motif around 960-Tyr residue of the insulin receptor binds to the N-terminal PTB domain of Shc. Subsequently, the 52-kDa, and, to a lesser extent, the 46-kDa Shc isoforms are tyrosine phosphorylate...
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The Src homology and collagen protein (Shc) is tyrosine phosphorylated in response to insulin; however, evidence for its interaction with insulin receptor (IR) in normal tissues is missing. Interactions between IR, Shc and regulatory subunits of the phosphatidylinositol 3'-kinase (PI 3'-kinase) were characterized in the present study in liver and muscles of chickens submitted to various nutriti...
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Insulin signaling at target tissues is essential for growth and development and for normal homeostasis of glucose, fat, and protein metabolism. Control over this process is therefore tightly regulated. It can be achieved by a negative feedback control mechanism whereby downstream components inhibit upstream elements along the insulin-signaling pathway (autoregulation) or by signals from apparen...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)53382-2