Skip to Main content Skip to Navigation
Journal articles

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

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.
Document type :
Journal articles
Complete list of metadata

https://hal-cnrs.archives-ouvertes.fr/hal-03028946
Contributor : Isabelle Tratner Connect in order to contact the contributor
Submitted on : Friday, November 27, 2020 - 6:39:58 PM
Last modification on : Wednesday, January 6, 2021 - 11:34:02 AM

Links full text

Identifiers

Collections

Citation

I Tratner, R Ofir, I Verma. Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential.. Molecular and Cellular Biology, American Society for Microbiology, 1992, 12 (3), pp.998-1006. ⟨10.1128/mcb.12.3.998⟩. ⟨hal-03028946⟩

Share

Metrics

Record views

14