Insulin stimulates the phosphorylation of ribosomal protein S6 in a cell-free system derived from 3T3-L1 adipocytes

O. M. Rosen, C. S. Rubin, M. H. Cobb, C. J. Smith

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Physiological concentrations of insulin stimulate the incorporation of 32P into ribosomal protein S6 in intact 3T3-L1 adipocytes. Extracts from cells treated with insulin also exhibit an increased ability to incorporate 32P from [γ-32P]ATP into protein S6 in vitro. The authors now report that the direct addition of insulin to particulate preparations containing high affinity insulin receptors and ribosomes derived from insulin-sensitive cells (not previously exposed to insulin) stimulates incorporation of 32P from [γ-32P]ATP into ribosomal protein S6 1.5- to 3.0-fold. The stimulation occurs at the same concentrations of insulin (0.1-1.0 nM) and within the same period of time as it does in intact cells.

Original languageEnglish (US)
Pages (from-to)3630-3636
Number of pages7
JournalJournal of Biological Chemistry
Volume256
Issue number8
StatePublished - Dec 1 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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