First Author | Fueller J | Year | 2008 |
Journal | Biochem Biophys Res Commun | Volume | 370 |
Issue | 4 | Pages | 552-6 |
PubMed ID | 18402774 | Mgi Jnum | J:134669 |
Mgi Id | MGI:3789513 | Doi | 10.1016/j.bbrc.2008.03.141 |
Citation | Fueller J, et al. (2008) C-RAF activation promotes BAD poly-ubiquitylation and turn-over by the proteasome. Biochem Biophys Res Commun 370(4):552-6 |
abstractText | BAD, a member of the BCL2 family, exhibits an original mode of regulation by phosphorylation. In the present report, we examine the role of the kinase C-RAF in this process. We show that the inducible activation of C-RAF promotes the rapid phosphorylation of BAD on Serine-112 (Ser-75 in the human protein), through a cascade involving the kinases MEK and RSK. Our findings reveal a new aspect of the regulation of BAD protein and its control by the RAF pathway: we find that C-RAF activation promotes BAD poly-ubiquitylation in a phosphorylation-dependent fashion, and increases the turn-over of this protein through proteasomal degradation. |