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Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine.

Year: 1982

Type: article

Abstract: Rat hepatoma cells were labeled with [32P]orthophosphate and the insulin receptor subunits were identified by immunoprecipitation and sodium dodecyl sulfate-acrylamide gel electrophoresis. In the basal state, only the Mr = 95,000 (beta) subunit of the insulin receptor was phosphorylated. The covalent labeling with 32P of this subunit was stimulated about 3-fold by insulin (10(-6) M). This stimulation was due to an increase in the content of phosphoserine, the appearance of phosphotyrosine, and a possible increase in phosphothreonine as well. These results suggest phosphorylation of the insulin receptor at multiple sites is an early event in insulin action.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(18)33955-3

Authors: M Kasuga, Y Zick, D L Blith, F A Karlsson, H U Häring, C R Kahn

Institutions: Brigham and Women's Hospital, Joslin Diabetes Center, National Institutes of Health, Harvard University, National Institute of Diabetes and Digestive and Kidney Diseases, National Cancer Institute

Language: English

Topic: Metabolism, Diabetes, and Cancer

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1538276446

FWCI: 21.44

Cites: 28

Cited by: 436

Related to: 10