Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential

I. Tratner, R. Ofir, I. M. Verma

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

We have studied the phosphorylation of the nuclear oncoprotein Fos by cyclic AMP-dependent protein kinase (PKA). We demonstrate that the human c- Fos protein, phosphorylated either in vitro with purified PKA or in vivo in JEG3 cells following treatment with forskolin, has similar phosphotryptic peptide maps. Serine 362, which constitutes part of a canonical PKA phosphorylation site (RKGSSS), is phosphorylated both in vivo and in vitro. A mutant of Fos protein in which serine residues 362 to 364 have been altered to alanine residues is not efficiently phosphorylated in vitro. Furthermore, Fos protein in which serines 362 to 364 have been altered to alanine shows increased transforming potential. We propose that phosphorylation of Fos by PKA is an important regulatory step in controlling its activity in normal cell growth and differentiation.

Original languageEnglish
Pages (from-to)998-1006
Number of pages9
JournalMolecular and Cellular Biology
Volume12
Issue number3
DOIs
StatePublished - 1 Jan 1992
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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