Insulin binds to and promotes the phosphorylation of a M r 210 000 component of its receptor in detergent extracts of rat liver microsomes
- 25 July 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 158 (2) , 243-246
- https://doi.org/10.1016/0014-5793(83)80587-0
Abstract
Insulin in the presence of Mn2+ and [γ32P]ATP promoted the phosphorylation of two proteins of M r 95 000 and M r 210 000 in detergent extracts of rat liver microsomes. The M r 210 000 protein was identified as a component of the insulin receptor by immunoprecipitation. It also bound [125I]insulin specifically, was phosphorylated largely on a tyrosine residue and could not be cleaved to smaller subunits under extreme reducing conditions. The M r 210 000 protein appears to be a component of a sub-population of liver membrane insulin receptors in which insulin-binding and insulin-stimulated tyrosine kinase phosphorylation site(s) reside in a single polypeptide chain.Keywords
This publication has 7 references indexed in Scilit:
- Receptor-mediated phosphorylation of the hepatic insulin receptor: Evidence that the M r 95,000 receptor subunit is its own kinaseProceedings of the National Academy of Sciences, 1983
- Insulin Receptor: Evidence That It Is a Protein KinaseScience, 1983
- Latent insulin receptors and possible receptor precursors in 3T3-L1 adipocytes.Proceedings of the National Academy of Sciences, 1983
- Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta.Proceedings of the National Academy of Sciences, 1982
- Purification and characterization of epidermal growth factor receptor/protein kinase from normal mouse liver.Proceedings of the National Academy of Sciences, 1982
- Preliminary characterization of a heat-stable protein from rat adipose tissue whose phosphorylation is stimulated by insulinBiochemical Journal, 1982
- Insulin Stimulates the Phosphorylation of the 95,000-Dalton Subunit of Its Own ReceptorScience, 1982