Substrate specificities of insulin and epidermal growth factor receptor kinases

Harald H. Klein, Gary R. Freidenberg, Renzo Cordera, Jerrold M. Olefsky

Research output: Contribution to journalArticlepeer-review


The abilities of insulin and EGF stimulated protein kinases to phosphorylate a series of exogenous substrates were compared using wheat germ lectin purified preparations of solubilized rat liver membranes. Three different kinds of substrates were found: substrates phosphorylated primarily by insulin stimulated kinase, substrates phosphorylated primarily by EGF stimulated kinase and substrates phosphorylated by both kinases to a similar extent. These results indicate that the insulin and the EGF receptor kinase have different, but overlapping, substrate specificities. In vivo, phosphorylation of cellular proteins by various hormone receptor kinases may be part of the signal transmission process for actions of the hormones. Different substrate specificities of kinases of different hormone receptors may therefore represent an important mechanism to preserve the specificity of the hormonal signal at the post receptor level.

Original languageEnglish
Pages (from-to)254-263
Number of pages10
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - Feb 28 1985

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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