A similar ribosomal protein S6 kinase activity is found in insulin-treated 3T3-L1 cells and chick embryo fibroblasts transformed by Rous sarcoma virus

Melanie H. Cobb, John G. Burr, Maurine E. Linder, Teri B. Gray, Jill S. Gregory

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Insulin and transformation by Rous sarcoma virus stimulate the phosphorylation of ribosomal protein S6. Soluble fractions containing activated S6 protein kinase from insulin-treated cells and from transformed chick embryo fibroblasts were compared. Based upon several characteristics notably elution from DEAE-cellulose and sedimentation in glycerol gradients, these two S6 protein kinase activities appear to be similar enzymes. Thus insulin and retroviral transformation may activate the same enzyme to regulate the phosphorylation state of S6.

Original languageEnglish (US)
Pages (from-to)702-708
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume137
Issue number2
DOIs
StatePublished - Jun 13 1986

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'A similar ribosomal protein S6 kinase activity is found in insulin-treated 3T3-L1 cells and chick embryo fibroblasts transformed by Rous sarcoma virus'. Together they form a unique fingerprint.

  • Cite this