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Vaux, David L.
Biochimica et biophysica acta, April 2011, 2011-Apr, 2011-04-00, Letnik: 1813, Številka: 4Journal Article
When cells kill themselves, they usually do so by activating mechanisms that have evolved specifically for that purpose. These mechanisms, which are broadly conserved throughout the metazoa, involve two processes: activation in the cytosol of latent cysteine proteases (termed caspases), and disruption of mitochondrial functions. These processes are linked in a number of different ways. While active caspases can cleave proteins in the mitochondrial outer membrane, and cleave and thereby activate certain pro-apoptotic members of the Bcl-2 family, proteins released from the mitochondria can trigger caspase activation and antagonise IAP family proteins. This review will focus on the pro-apoptotic molecules that are released from the mitochondria of cells endeavouring to kill themselves. This article is part of a Special Issue entitled Mitochondria: the deadly organelle. ► Proteins are released from mitochondria during apoptosis. ► Several of these proteins can bind to IAPs, but they do not appear to be important regulators of cell death. ► During apoptosis, cytochrome c released from mitochondria is essential for activation of Apaf-1, which in turn activates caspases. ► AIF and endoG are released from mitochondria during apoptosis, but this is neither sufficient nor required for cell death.
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