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Apoptosis

Death cycle and Swiss army knives

Nature volume 391, pages 441–442 (1998)Cite this article

Cytochrome c leads a double life. When a cell is called on to commit apoptotic suicide, cytochrome c relocalizes from the mitochondria to the cytosol. There, it helps to activate the foot-soldiers of apoptosis — the death proteases known as caspases1. How cytochrome c escapes from the mitochondria is still a matter of debate1, but it is clear that certain elements within the apoptotic regulatory hierarchy do not condone such behaviour. In particular, overexpression of the cell-death suppressors Bcl-2 and Bcl-xL prevents the release of cytochrome c, suggesting that these proteins act upstream of cytochrome c in the pathway to cell death2,3. However, on pages 449 and 496 of this issue, Zhivotovsky et al.4 and Rossé et al.5 show that Bcl-2 can also protect cells downstream of cytochrome c release, forcing a re-evaluation of this newly acquired dogma.

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Figure 1: Models for the function of Bcl-2 in apoptosis.

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  1. Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, 11724, New York, USA

    Michael O. Hengartner

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  1. Michael O. Hengartner
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Hengartner, M. Death cycle and Swiss army knives. Nature 391, 441–442 (1998). https://doi.org/10.1038/35036

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