Insulin rapidly stimulates tyrosine phosphorylation of a Mr-185,000 protein in intact cells
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Summary
Ppl85 is maximal within seconds after exposure of the cells to insulin and exhibits a dose–response curve similar to that of receptor autophosphorylation, suggesting that this protein represents the endogenous substrate for the insulin receptor kinase.
- Type
- article
- Published
- 1985-11-14
- Cited by
- 574
- References
- 31
- OpenAlex
- https://openalex.org/W1984159784
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4285981
Keywords
Autophosphorylation, IRS2, Insulin receptor, Tyrosine phosphorylation, Insulin receptor substrate
References
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- The insulin-stimulated receptor kinase is a tyrosine-specific casein kinase.
- Dedifferentiated variants of a rat hepatoma: Analysis by cell hybridization
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- Three glycolytic enzymes are phosphorylated at tyrosine in cells transformed by Rous sarcoma virus
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system
- Insulin-like effect of vanadate on adipocyte glycogen synthase and on phosphorylation of 95,000 dalton subunit of insulin receptor.
Cited by
- Antiphosphotyrosine immunoprecipitation of an insulin-stimulated receptor phosphatase activity from FRTL5 cells.
- Regulation of protein phosphorylation by insulin and insulin-like growth factors in cultured fetal neurons.
- Phosphorylation of cellular proteins in Rous sarcoma virus-infected cells: analysis by use of anti-phosphotyrosine antibodies
- Insulin-Receptor Kinase Activity of Adipose Tissue From Morbidly Obese Humans With and Without NIDDM
- A novel sulfotransferase sulfates tyrosine-containing peptides and proteins.
- Effect of glucagon on insulin receptor substrate‐1 (IRS‐1) phosphorylation and association with phosphatidylinositol 3‐kinase (PI 3‐kinase)
- Interleukin 4 receptor: signaling mechanisms.
- Deletion of exon 21 of the insulin receptor eliminates tyrosine kinase activity but preserves mitogenic signaling.
- Phosphorylation of Insulin Receptor Substrate-1 on Multiple Serine Residues, 612, 632, 662, and 731, Modulates Insulin Action (*)
- Insulin receptor-induced phosphorylation of cellular and synthetic substrates is regulated by the receptor beta-subunit C-terminus.
- Disruption of insulin receptor substrate 2 causes type 2 diabetes because of liver insulin resistance and lack of compensatory beta-cell hyperplasia.
- Insulin activates ATP-sensitive K(+) channels in pancreatic beta-cells through a phosphatidylinositol 3-kinase-dependent pathway.
- Insulin Substrate Receptor (IRS) proteins in normal and malignant hematopoiesis
- Cytosolic substrates for the insulin receptor kinase.
- Detection of insulin and insulin-like growth factors I and II in saliva and potential synthesis in the salivary glands of mice. Effects of type 1 diabetes mellitus.
- Generation and use of anti-phosphotyrosine antibodies for immunoblotting.
- Mutations in the insulin receptor gene in genetic forms of insulin resistance.
- Endogenous substrates of the insulin receptor: studies with cells expressing wild-type and mutant receptors.
- Protein phosphorylation and insulin action.
- Factors affecting insulin-regulated hepatic gene expression.
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