In Vitro Binding and Phosphorylation of Insulin Receptor Substrate 1 by the Insulin Receptor : Role of Interactions Mediated by the Phosphotyrosine-Binding Domain and the Pleckstrin-Homology Domain
✍ Scribed by Jonathan M. Backer; Christina Wjasow; Yitao Zhang
- Book ID
- 115133761
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 693 KB
- Volume
- 245
- Category
- Article
- ISSN
- 1432-1327
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Insulin receptors are disulfide-linked oligotetramers composed of two heterodimers each containing a 130-kDa 01 subunit and a 90-kDa p subunit. Insulin binds to the extracellular 01 subunit, and in the process stimulates the autophosphorylation of the p subunit and the expression of tyrosine kinase
## Abstract The insulin receptor substrate‐1 (IRS‐1), a docking protein for both the insulin (InR) and the insulin‐like growth factor‐1 (IGF‐IR) receptors, sends a mitogenic, anti‐differentiation and transforming signal. We now show that down‐regulation of IRS‐1 in cells transformed by v‐src revers
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