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

Biochemical and Biophysical Research Communications
Jochen FuellerAntoine Galmiche

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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Citations

Oct 11, 2008·Cell Death and Differentiation·K Balmanno, S J Cook
Jul 23, 2011·Genes & Cancer·David MatallanasWalter Kolch
Oct 21, 2011·Apoptosis : an International Journal on Programmed Cell Death·Leonardo RomoriniSantiago G Miriuka
Jan 1, 2012·FEBS Open Bio·Zhanxiang Wang, Debbie C Thurmond
Apr 21, 2012·Seminars in Cell & Developmental Biology·Albert NeutznerMariusz Karbowski
Dec 17, 2011·Biochemical and Biophysical Research Communications·Eric TrécherelAntoine Galmiche
Jan 6, 2009·Biochimica Et Biophysica Acta·Leonardo RomoriniAdali Pecci
Nov 10, 2009·Advances in Enzyme Regulation·Lisa PolzienUlf R Rapp
May 27, 2017·The FEBS Journal·Simon J CookMatthew J Sale
Jul 22, 2010·Molecular Cancer Research : MCR·Antoine GalmicheDenis Chatelain

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BCL-2 Family Proteins

BLC-2 family proteins are a group that share the same homologous BH domain. They play many different roles including pro-survival signals, mitochondria-mediated apoptosis and removal or damaged cells. They are often regulated by phosphorylation, affecting their catalytic activity. Here is the latest research on BCL-2 family proteins.