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Approaches to the molecular cloning of protein-tyrosine phosphatases in insulin-sensitive tissues

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Abstract

The intrinsic tyrosyl kinase activity of the insulin receptor is regulated by a balance between insulin-induced receptor autophosphorylation, which stimulates the receptor kinase, and enzymatic dephosphorylation of the receptor, which deactivates its kinase activity. The cellular protein-tyrosine phosphatase (PTPase) enzymes responsible for reversing the activated state of the insulin receptor have not been characterized. Our laboratory is interested in identifying and cloning the specific PTPase(s) that regulate the phosphorylation state of the insulin receptor. This chapter will summarize the design and results of our initial molecular cloning studies to identify specific PTPases in insulin-sensitive tissues that may have a potential physiological role in insulin action and clinical insulin resistance.

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Authors and Affiliations

  1. Research Division, Joslin Diabetes Center and Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 02215, Boston, MA, USA

    Barry J. Goldstein, Wei-Ren Zhang, Naotake Hashimoto & C. Ronald Kahn

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  1. Barry J. Goldstein
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  2. Wei-Ren Zhang
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  3. Naotake Hashimoto
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  4. C. Ronald Kahn
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Goldstein, B.J., Zhang, WR., Hashimoto, N. et al. Approaches to the molecular cloning of protein-tyrosine phosphatases in insulin-sensitive tissues. Mol Cell Biochem 109, 107–113 (1992). https://doi.org/10.1007/BF00229763

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