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  • Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10.

Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10.

Nature (2001-04-20)
S H Chiang, C A Baumann, M Kanzaki, D C Thurmond, R T Watson, C L Neudauer, I G Macara, J E Pessin, A R Saltiel
摘要

The stimulation of glucose uptake by insulin in muscle and adipose tissue requires translocation of the GLUT4 glucose transporter protein from intracellular storage sites to the cell surface. Although the cellular dynamics of GLUT4 vesicle trafficking are well described, the signalling pathways that link the insulin receptor to GLUT4 translocation remain poorly understood. Activation of phosphatidylinositol-3-OH kinase (PI(3)K) is required for this trafficking event, but it is not sufficient to produce GLUT4 translocation. We previously described a pathway involving the insulin-stimulated tyrosine phosphorylation of Cbl, which is recruited to the insulin receptor by the adapter protein CAP. On phosphorylation, Cbl is translocated to lipid rafts. Blocking this step completely inhibits the stimulation of GLUT4 translocation by insulin. Here we show that phosphorylated Cbl recruits the CrkII-C3G complex to lipid rafts, where C3G specifically activates the small GTP-binding protein TC10. This process is independent of PI(3)K, but requires the translocation of Cbl, Crk and C3G to the lipid raft. The activation of TC10 is essential for insulin-stimulated glucose uptake and GLUT4 translocation. The TC10 pathway functions in parallel with PI(3)K to stimulate fully GLUT4 translocation in response to insulin.

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Rac/cdc42检测试剂(PAK1 PBD,琼脂糖),300 µg, Specifically binds to & precipitates Rac-GTP & cdc42-GTP from cell lysates. For use in Affinity Binding Assays.
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