Identification of SHC as a Substrate of the Insulin Receptor Kinase Distinct from the GAP-Associated 62-kDa Tyrosine Phosphoprotein
| Autor: | Richard A. Roth, Kristina S. Kovacina |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Time Factors
Biophysics CHO Cells environment and public health Biochemistry Receptor tyrosine kinase Phosphates Substrate Specificity chemistry.chemical_compound Cricetinae Insulin receptor substrate Animals Insulin Sulfhydryl Compounds Phosphotyrosine Molecular Biology biology GRB10 GTPase-Activating Proteins Autophosphorylation Antibodies Monoclonal Proteins Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Phosphoproteins Molecular biology Receptor Insulin IRS2 Kinetics Insulin receptor chemistry ras GTPase-Activating Proteins ROR1 biology.protein Tyrosine biological phenomena cell phenomena and immunity hormones hormone substitutes and hormone antagonists |
| Zdroj: | Biochemical and Biophysical Research Communications. 192:1303-1311 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1993.1558 |
| Popis: | Insulin stimulated tyrosine phosphorylation of SHC, a SH2 containing protein, was demonstrated in Chinese hamster ovary cellsoverexpressing the insulin receptor by immunoblotting with antiphosphotyrosine antibodies and in vivo labeling. Insulin induced tyrosine phosphorylation of SHC occurred very rapidly (within 1 min) with a dose curve which paralleled the autophosphorylation of the insulin receptor. Phosphorylation of SHC appeared to occur to a high stoichiometry since insulin induced the majority of SHC to shift to a higher molecular weight.The tyrosine phosphorylated SHC was not bound by the GTPase activating protein of Ras although a distinct 62 kDa tyrosine phosphorylated protein was found to be associated in the same experiments. It also was not bound to the insulin receptor, phosphatidylinositol 3-kinase or insulin receptor substrate-1. |
| Databáze: | OpenAIRE |
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