Format

Send to

Choose Destination
Biochem Biophys Res Commun. 1994 Jun 15;201(2):740-7.

Phosphorylation of c-Raf-1 by protein kinase A interferes with activation.

Author information

1
Max-Planck-Institut fuer Molekulare Genetik, Abt. Schuster, Berlin (Dahlem), FRG.

Abstract

c-Raf-1 is a serine/threonine-specific protein kinase which is regulated by phosphorylation. A putative c-AMP dependent protein kinase PKA phosphorylation site with the consensus sequence RRXS, Ser43, and a predominant phosphorylation site of c-Raf-1, Ser259, can be phosphorylated by PKA in vitro as shown by comparison of phosphopeptide maps of recombinant wild-type c-Raf-1 and the corresponding mutants. In vivo stimulation of the PKA pathway by treatment of A431 cells with Forskolin results in increase of phosphorylation in Ser43. Forskolin reduces the upshift of c-Raf-1 induced by EGF-treatment. It inhibits the EGF-activation of the c-Raf-1 protein kinase activity tested in vitro with a peptide substrate.

PMID:
8003010
DOI:
10.1006/bbrc.1994.1763
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center