Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis

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VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria.

Truncated BID (tBID), a proapoptotic BCL2 family protein, induces BAK/BAX-dependent release of cytochrome c and other mitochondrial intermembrane proteins to the cytosol to induce apoptosis. The voltage-dependent anion channels (VDACs) are the primary gates for solutes across the outer mitochondrial membrane (OMM); however, their role in apoptotic OMM permeabilization remains controversial. Her...

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Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.

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Apoptosis: it's BAK to VDAC.

The voltage-dependent anion channel (VDAC) of the mitochondrial outer membrane (MOM; Mannella & Kinnally, 2008)—also known as mitochondrial porin—has long been implicated in regulating the mitochondrial response to certain cell death stimuli (Galluzzi & Kroemer, 2007). This includes a potential role in MOM permeabilization (MOMP) during apoptosis, which is a necessary step in the release of cyt...

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The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release.

Cytochrome c release from mitochondria is a key event in apoptosis signaling that is regulated by Bcl-2 family proteins. Cleavage of the BH3-only protein Bid by multiple proteases leads to the formation of truncated Bid (tBid), which, in turn, promotes the oligomerization/insertion of Bax into the mitochondrial outer membrane and the resultant release of proteins residing in the intermembrane s...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 2015

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.1510574112