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Publication : C-RAF activation promotes BAD poly-ubiquitylation and turn-over by the proteasome.

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.
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