Novel C-Raf phosphorylation sites: serine 296 and 301 participate in Raf regulation.
FEBS Lett
; 579(2): 464-8, 2005 Jan 17.
Article
em En
| MEDLINE
| ID: mdl-15642359
ABSTRACT
The C-Raf kinase is regulated by numerous phosphorylation steps. To quantify the most prominent phosphorylation sites of C-Raf, we performed mass spectrometry analysis of wild-type C-Raf and the constitutively active C-Raf mutant C-Raf-Y340D/Y341D. We confirmed phosphorylation of most of the sites reported in the literature with the exception that we did not detect phosphorylation of threonine 268/269 (autophosphorylation sites) and threonine 491/serine 494 (kinase activation loop). Importantly, we detected novel phosphorylation sites at the positions of serine 296 and 301. The degree of phosphorylation in these positions depends on the level of activation of C-Raf. Furthermore, we show here, using point mutant forms of C-Raf kinases with serine to alanine and serine to aspartic acid substitution, that serines 296 and 301 contribute to negative regulation of C-Raf.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Serina
/
Proteínas Proto-Oncogênicas c-raf
Limite:
Animals
/
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2005
Tipo de documento:
Article
País de afiliação:
Alemanha