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

被引:335
作者
Djavaheri-Mergny, M. [1 ,2 ]
Maiuri, M. C. [3 ,4 ]
Kroemer, G. [3 ,4 ]
机构
[1] INSERM, VINCO U916, Inst Bergonie, F-33076 Bordeaux, France
[2] Univ Bordeaux, Bordeaux, France
[3] Inst Gustave Roussy, INSERM, U848, F-94805 Villejuif, France
[4] Univ Paris 11, Villejuif, France
关键词
Beclin; 1; autophagy; apoptosis; BCL-2;
D O I
10.1038/onc.2009.519
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. Oncogene (2010) 29, 1717-1719; doi:10.1038/onc.2009.519; published online 25 January 2010
引用
收藏
页码:1717 / 1719
页数:3
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