What Do Receptor Kinases Do?

  • Paul F. Pilch
  • Michael A. Shia
  • Joshua B. Rubin


There is now compelling evidence that the β subunit of the insulin receptor is an insulin-regulated, tyrosine-specific protein kinase. Some of this evidence is detailed in the previous chapters of this volume (Chapter 4). Data from our own laboratory on this point include the following observations: (1) Affinity-purified insulin receptor is capable of ligand-dependent autophosphorylation as well as kinase activity toward exogenous substrates.(1) (2) An immunoprecipitate of partially purified insulin receptor retains kinase activity.(2) (3) The β subunit of the receptor has an adenosine triphosphate (ATP) binding site.(2) (4) Treatment of purified receptor with elastase abolishes kinase activity concomitant with cleavage of the β subunit. Elastase action has no effect on insulin binding to the α subunit nor does it alter the structure of the α subunit.(1) Similar studies from several laboratories have given essentially identical results on one or more aspects of the above considerations.(3–6) It thus seems highly likely that tyrosine-specific protein kinase activity is an intrinsic property of the insulin receptor and is not due to the action of an unseen but tightly receptor-associated protein.


Kinase Activity Insulin Receptor Insulin Binding Rous Sarcoma Virus Elastase Action 


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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Paul F. Pilch
    • 1
  • Michael A. Shia
    • 1
  • Joshua B. Rubin
    • 1
  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA

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