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Specific Activation of the Insulin Receptor by the Transmembrane Domain Peptides

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Peptides: The Wave of the Future

Part of the book series: American Peptide Symposia ((APSY,volume 7))

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Abstract

The binding of insulin to the extracellular domain of the insulin receptor (IR) triggers activation of tyrosine kinase and transmits the signal to the downstream signaling cascade [1]. However, it is still unknown how insulin binding to the extracellular binding site causes receptor activation. Several studies using IR mutants have investigated the function of the transmembrane domain (TMD) in the receptor activation process, and it was suggested that the TMD might have some role in the receptor activation [2,3]. We report here a different approach using a synthetic peptide corresponding to the TMD of IR (IR-TM), to investigate the role of TMD in receptor activation.

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References

  1. Lee, J., Pilch, P.F. Am. J. Physiol. Cell Physiol. 266, C319 (1994).

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© 2001 Springer Science+Business Media Dordrecht

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Miyazaki, M., Lee, J., Shibue, M., Fujiura, T., Maeda, H., Shoelson, S.E. (2001). Specific Activation of the Insulin Receptor by the Transmembrane Domain Peptides. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_427

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  • DOI: https://doi.org/10.1007/978-94-010-0464-0_427

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-3905-5

  • Online ISBN: 978-94-010-0464-0

  • eBook Packages: Springer Book Archive

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