[Mechanism of insulin action--signal transductions after binding to insulin receptor] - PubMed

[Article in Japanese]

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• PMID: 8282127
• DOI: 10.1507/endocrine1927.69.10_1029

Review

[Mechanism of insulin action--signal transductions after binding to insulin receptor]

[Article in Japanese]

M Kasuga. Nihon Naibunpi Gakkai Zasshi. 1993.

Abstract

Insulin binds to the alpha subunit of the insulin receptor which activates the tyrosine kinase in the beta subunit and tyrosine-phosphorylates the insulin receptor substrates-1 (IRS-1). Insulin promotes the formation of a complex between tyrosine-phosphorylated IRS-1 and several proteins including phosphoinositide(PI) 3-kinase, a heterodimer consisting of regulatory 85-kDa (p85) and catalytic 110-kDa (p110) subunits, GRB2 and Syp via the Src homology region 2 (SH2) domains. Recently, it was suggested that GRB2-Sos complex binding to IRS-1 was linked to Ras activation and that PI 3-kinase binding to IRS-1 was linked to activation of glucose transport. Since the mechanism of insulin-stimulated glucose uptake is mainly due to translocation of glucose transporters from an intracellular vesicle pool to the plasma membrane, PI 3-kinase activity may be involved in vesicle transport in mammalian cells.

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