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Role of binding proteins to IRS-1 in insulin signalling

  • Chapter
Insulin Action

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 24))

Abstract

Insulin elicits its divergent metabolic and mitogenic effects by binding to its specific receptor, which belongs to the family of receptor tyrosine kinases. The activated insulin receptor phosphorylates the intracellular substrate IRS-1, which then binds various signalling molecules that contain SRC homology 2 domains, thereby propagating the insulin signal. Among these IRS-1-binding proteins, the Grb2-Sos complex and the protein tyrosine Phosphatase SHP-2 transmit mitogenic signals through the activation of Ras, and phosphoinositide 3-kinase is implicated in the major metabolic actions of insulin. Although substantial evidence indicates the importance of IRS-1 in insulin signal transduction, the generation of IRS-1-deficient mice has revealed the existence of redundant signalling pathways. (Mol Cell Biochem 182: 13-22, 1998)

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Authors and Affiliations

  1. Second Department of Internal Medicine, Kobe University School of Medicine, Kobe, Japan

    Wataru Ogawa, Takashi Matozaki & Masato Kasuga

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  1. Wataru Ogawa
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  2. Takashi Matozaki
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  3. Masato Kasuga
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  1. Centre Hospitalier de l’Université de Montreal Pavillion Hotel Dieu, 3840, Rue Saint-Urbain, Montreal, Quebec, H2W 1T8, Canada

    Ashok K. Srivastava

  2. Polypeptide Hormone Laboratory Strathcona Anatomy & Dentistry Building, 3640 University Street, Room W3, 15, Montreal, Quebec, H3A 2B2, Canada

    Barry I. Posner

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© 1998 Springer Science+Business Media Dordrecht

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Ogawa, W., Matozaki, T., Kasuga, M. (1998). Role of binding proteins to IRS-1 in insulin signalling. In: Srivastava, A.K., Posner, B.I. (eds) Insulin Action. Developments in Molecular and Cellular Biochemistry, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5647-3_2

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  • DOI: https://doi.org/10.1007/978-1-4615-5647-3_2

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