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Apoptosis without caspases?

Caspases are often thought of as fundamental to apoptosis: they function in the death receptor pathway and stress-induced apoptosis and cleave targets that directly promote cell death. But what about caspase-independent mechanisms? In a Commentary on p. 4727, Guido Kroemer and co-workers examine the role of apoptosis-inducing factor (AIF), a mitochondrial flavoprotein that might drive caspase-independent apoptosis. Apoptotic signalling causes AIF to translocate from mitochondria to the nucleus, where it binds to DNA, causes it to fragment and induces cell death. Recent work has uncovered the mechanistic bases for the oxidoreductase and DNA-binding activities of AIF, revealing that its redox and apoptotic functions are separable. In addition, several studies have shown that translocation of AIF to the nucleus accompanies apoptosis in cells in which caspases are inhibited, knocked out or simply not activated. Furthermore, anti-AIF antibodies can sometimes prevent apoptosis when caspase inhibitors do not. Whether AIF is truly independent of caspases is still disputed. Indeed, Kroemer and co-workers suggest that crosstalk between AIF and caspases is likely. Nevertheless, evidence for the importance of this ancient protein in cell death is clearly mounting.

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Apoptosis-inducing factor (AIF): key to the conserved caspase-independent pathways of cell death?

Céline Candé, Francesco Cecconi, Philippe Dessen, and Guido Kroemer
JCS 2002 115: 4727-4734. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?