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Insulin Receptor: Aspects of its Structure and Function

  • Chapter
New Concepts in the Pathogenesis of NIDDM

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 334))

Abstract

Insulin receptors are composed of two 130-kDa α subunits and two 90-kDa β subunits which are linked by disulfide bonds forming a heterotetrameric structure (see reviews by Czech1, and Goldfine2). The two subunits are synthesized as a single-chain precursor protein encoded by 22 exons3. The α subunit, extracellularly located, is anchored to the cell membrane by disulfides to the β subunit which contains a putative trans-membrane domain4. Photoaffinity labeling with light-sensitive insulin photoprobes5 and chemical crosslinking6 have established that insulin binds to the extracellular α subunit. Insulin binding causes the autophosphorylation of the insulin receptor β subunit, the latent tyrosine kinase activity of which is thus stimulated as a consequence. The activation of insulin receptor kinase activity initiates a cascade of intra-cellular protein phosphorylation which regulates the cellular metabolic and mitogenic activity in response to insulin (see reviews by Goldfine2 and by Rosen7). Studies of the effect on the cellular response to insulin in mutant receptors in which the intracellular β subunit has been modified by site-mutagenesis or sequence deletion have demonstrated the domain related multifunctional nature of the insulin receptor (see review by Olefsky8).

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Authors and Affiliations

  1. Banting and Best Department of Medical Research, University of Toronto, Toronto, Ont., Canada, M5G 1L6

    Cecil C. Yip

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  1. Cecil C. Yip
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Editors and Affiliations

  1. Karolinska Hospital, Stockholm, Sweden

    Claes Göran Östenson  & Suad Efendić  & 

  2. University of Toronto, Toronto, Ontario, Canada

    Mladen Vranic

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© 1993 Springer Science+Business Media New York

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Yip, C.C. (1993). Insulin Receptor: Aspects of its Structure and Function. In: Östenson, C.G., Efendić, S., Vranic, M. (eds) New Concepts in the Pathogenesis of NIDDM. Advances in Experimental Medicine and Biology, vol 334. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2910-1_6

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  • DOI: https://doi.org/10.1007/978-1-4615-2910-1_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6262-3

  • Online ISBN: 978-1-4615-2910-1

  • eBook Packages: Springer Book Archive

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