Substrates for Insulin-Receptor Kinase
| Autor: | K Momomura, Yuko Tashiro-Hashimoto, Masato Kasuga, Teruo Shiba, Takashi Kadowaki, Tetsuro Izumi, Kazuyuki Tobe |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Protein Conformation
Endocrinology Diabetes and Metabolism macromolecular substances Protein tyrosine phosphatase SH2 domain Receptor tyrosine kinase Substrate Specificity MAP2K7 chemistry.chemical_compound Internal Medicine Animals Humans Medicine Phosphorylation Advanced and Specialized Nursing biology business.industry Cell Membrane Tyrosine phosphorylation Protein-Tyrosine Kinases Receptor Insulin IRS2 Cell biology Models Structural Insulin receptor chemistry biology.protein business Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Diabetes Care. 13:317-326 |
| ISSN: | 1935-5548 0149-5992 |
| DOI: | 10.2337/diacare.13.3.317 |
| Popis: | Several studies suggest that the tyrosine-specific protein kinase activity of the β-subunit of the insulin receptor is necessary to mediate the biological effects of insulin. This conclusion leads to the hypothesis that the effect of insulin is mediated through the tyrosine phosphorylation of cellular substrates by the insulin-receptor tyrosine kinase. In this review, the experimental evidence regarding insulin-stimulated phosphorylation of proteins both in vitro and in vivo is evaluated. In a cell-free system, tubulin, microtubuleassociated protein 2, tau, fodrin, calmodulin-dependent kinase, calmodulin, and lipocortins 1 and 2 were reported to be good substrates for insulin-receptor kinase. However, none were found to be tyrosine phosphorylated in an intact-cell system. In intact-cell systems, proteins of M, 185,000 (pp185), 120,000 (pp120), 240,000 (pp240), 15,000 (pp15), 60,000 (pp60), and 62,000 (pp62) as well as several others were reported to be tyrosine phosphorylated in an insulin-dependent fashion. However, the function or functional alteration of these proteins induced by insulin-stimulated tyrosine phosphorylation is not clear. Therefore, physiologically relevant substrates for the insulin-receptor kinase have not been established, and more work is necessary to verify the phosphorylation cascade hypothesis of insulin action. |
| Databáze: | OpenAIRE |
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