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  • Title: Insulin receptor autophosphorylation and exogenous substrate phosphorylation: role of receptor C-terminus and effects of mild reduction.
    Author: Clark S, Konstantopoulos N.
    Journal: Biochem Biophys Res Commun; 1994 Apr 15; 200(1):330-7. PubMed ID: 8166701.
    Abstract:
    A mutant insulin receptor lacking the final 69 amino acids of the beta-subunit (delta 69) was used to examine the role of the receptor C-terminal domain in kinase activation. With increasing deletion of the C-terminus from 43 to 69 amino acids we show that exogenous peptide kinase activity is lost before autokinase activity. Despite this, phosphorylation of an in vivo insulin receptor substrate, IRS-1, and insulin bioeffects are similar to wild-type. In addition, with the exception of insulin-stimulated peptide phosphorylation, the reductant glutathione modified kinase activity in a similar manner for both wild-type and mutant delta 69 receptors. These results suggest that conformational changes proposed to occur within the receptor C-terminus upon insulin binding may not be necessary for kinase activation under a variety of conditions.
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