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- W2136073669 endingPage "539" @default.
- W2136073669 startingPage "532" @default.
- W2136073669 abstract "The localization and control of Bcl-2 proteins on mitochondria is essential for the intrinsic pathway of apoptosis. Anti-apoptotic Bcl-2 proteins reside on the outer mitochondrial membrane (OMM) and prevent apoptosis by inhibiting the activation of the pro-apoptotic family members Bax and Bak. The Bcl-2 subfamily of BH3-only proteins can either inhibit the anti-apoptotic proteins or directly activate Bax or Bak. How these proteins interact with each other, the mitochondrial surface and within the OMM are complex processes we are only beginning to understand. However, these interactions are fundamental for the transduction of apoptotic signals to mitochondria and the subsequent release of caspase activating factors into the cytosol. In this review we will discuss our knowledge of how Bcl-2 proteins are directed to mitochondria in the first place, a crucial but poorly understood aspect of their regulation. This article is part of a Special Issue entitled Mitochondria: the deadly organelle." @default.
- W2136073669 created "2016-06-24" @default.
- W2136073669 creator A5003415888 @default.
- W2136073669 creator A5025751109 @default.
- W2136073669 creator A5036674251 @default.
- W2136073669 date "2011-04-01" @default.
- W2136073669 modified "2023-10-17" @default.
- W2136073669 title "Bcl-2 proteins and mitochondria—Specificity in membrane targeting for death" @default.
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