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

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• 作者：Jochen Fueller ; Matthias Becker ; Arnold R. Sienerth ; Andreas Fischer ; Christian Hotz ; Antoine Galmiche
• 关键词：BAD ; C-RAF ; Phosphorylation ; Ubiquitylation ; Proteasome
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2008
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：13 June 2008
• 卷：370
• 期：4
• 页码：552-556
• 文件大小：294 K

摘要

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.