Bcl-2 proteins and mitochondria-Specificity in membrane targeting for death

Jennefer Lindsay, Mauro Degli Esposti, Andrew P. Gilmore

    Research output: Contribution to journalArticlepeer-review


    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. © 2010 Elsevier B.V.
    Original languageEnglish
    Pages (from-to)532-539
    Number of pages7
    JournalBiochimica et Biophysica Acta - Molecular Cell Research
    Issue number4
    Publication statusPublished - Apr 2011


    • Apoptosis
    • Bax
    • Bcl-2
    • Bid
    • Membrane lipids
    • Mitochondria
    • MOMP
    • Tail-anchor sequence


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