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Review
. 2010 Mar 25;29(12):1717-9.
doi: 10.1038/onc.2009.519. Epub 2010 Jan 25.

Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1

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Review

Cross talk between apoptosis and autophagy by caspase-mediated cleavage of Beclin 1

M Djavaheri-Mergny et al. Oncogene. .

Erratum in

  • Oncogene. 2010 Dec 9;29(49):6508

Abstract

Beclin 1 has a key role in the initiation of autophagy, a process of self-cannibalism in which cytoplasmic constituents are sequestered and targeted for lysosomal degradation. In a recent issue of Cell Death & Disease, Wirawan et al. report the significant finding that caspases can cleave Beclin 1, thereby destroying its pro-autophagic activity. Moreover, the C-terminal fragment of Beclin 1 that results from this cleavage acquires a new function and can amplify mitochondrion-mediated apoptosis. Of note, the BH3 domain of Beclin 1 remains within the N-terminal fragment, which has no detectable pro-apoptotic activity. These findings provide important insights into the molecular cross talk between autophagy and apoptosis.

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