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 Citations (Scopus)

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

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Ribosomal Protein S6 Kinases
3T3-L1 Cells
Rous sarcoma virus
Chick Embryo
Fibroblasts
Viruses
Phosphorylation
Insulin
Protein Kinases
Ribosomal Protein S6
S 6
DEAE-Cellulose
Enzymes
Sedimentation
Glycerol
Cells

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A similar ribosomal protein S6 kinase activity is found in insulin-treated 3T3-L1 cells and chick embryo fibroblasts transformed by Rous sarcoma virus. / Cobb, Melanie H.; Burr, John G.; Linder, Maurine E.; Gray, Teri B.; Gregory, Jill S.

In: Biochemical and Biophysical Research Communications, Vol. 137, No. 2, 13.06.1986, p. 702-708.

Research output: Contribution to journalArticle

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