Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity

Morris F. White, James N. Livingston, Jonathan M. Backer, Vilma Lauris, Thomas J. Dull, Axel Ullrich, C. Ronald Kahn

Research output: Contribution to journalArticle

264 Scopus citations


Tyrosyl phosphorylation is implicated in the mechanism of insulin action. Mutation of the β-subunit of the insulin receptor by substitution of tyrosyl residue 960 with phenylalanine had no effect on insulin-stimulated autophosphorylation or phosphotransferase activity of the purified receptor. However, unlike the normal receptor, this mutant was not biologically active in Chinese hamster ovary cells. Furthermore, insulin-stimulated tyrosyl phosphorylation of at least one endogenous substrate (pp185) was increased significantly in cells expressing the normal receptor but was barely detected in cells expressing the mutant. Therefore, β-subunit autophosphorylation was not sufficient for the insulin response, and a region of the insulin receptor around Tyr-960 may facilitate phosphorylation of cellular substrates required for transmission of the insulin signal.

Original languageEnglish (US)
Pages (from-to)641-649
Number of pages9
Issue number5
Publication statusPublished - Aug 26 1988
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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