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VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis
Emily H.-Y. Cheng,1
Tatiana V. Sheiko,2
Jill K. Fisher,1
William J. Craigen,2
Stanley J. Korsmeyer1*
Abstract:
The multidomain proapoptotic molecules BAK or BAX are requiredto initiate the mitochondrial pathway of apoptosis. How cellsmaintain the potentially lethal proapoptotic effector BAK ina monomeric inactive conformation at mitochondria is unknown.In viable cells, we found BAK complexed with mitochondrial outer-membraneprotein VDAC2, a VDAC isoform present in low abundance thatinteracts specifically with the inactive conformer of BAK. Cellsdeficient in VDAC2, but not cells lacking the more abundantVDAC1, exhibited enhanced BAK oligomerization and were moresusceptible to apoptotic death. Conversely, overexpression ofVDAC2 selectively prevented BAK activation and inhibited themitochondrial apoptotic pathway. Death signals activate "BH3-only"molecules such as tBID, BIM, or BAD, which displace VDAC2 fromBAK, enabling homo-oligomerization of BAK and apoptosis. Thus,VDAC2, an isoform restricted to mammals, regulates the activityof BAK and provides a connection between mitochondrial physiologyand the core apoptotic pathway.
1 Howard Hughes Medical Institute, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA. 2 Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 770303498, USA.
* To whom correspondence should be addressed. E-mail: stanley_korsmeyer{at}dfci.harvard.edu
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