C-RAF activation promotes BAD poly-ubiquitylation and turn-over by the proteasome |
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Authors: | Fueller Jochen Becker Matthias Sienerth Arnold R Fischer Andreas Hotz Christian Galmiche Antoine |
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Institution: | Institut für Medizinische Strahlenkunde und Zellforschung (MSZ), University of Würzburg, Versbacher Strasse 5, D-97078, Würzburg, Germany |
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Abstract: | 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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Keywords: | 4-OHT 4-hydroxytamoxifene RSK ribosomal protein S6 kinase |
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