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Cancer Lett. 2009 Feb 8;274(1):95-100. doi: 10.1016/j.canlet.2008.09.004. Epub 2008 Oct 7.

Caspase-mediated cleavage of ATG6/Beclin-1 links apoptosis to autophagy in HeLa cells.

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Institute for Innovative Cancer Research, University of Ulsan College of Medicine and Asan Medical Center, Seoul 138-736, Republic of Korea.


Autophagy is a catabolic process involved in cell death and in cell protective mechanism. Autophagic cell death is differentiated from apoptosis by the presence of double or multiple-membrane enclosed vesicles, and the ATG proteins are essential for the formation of these autophagic vesicles. Here, we show that ATG6/Beclin-1 is a novel caspase substrate. ATG6 is directly cleaved by caspases in a process inhibited by the pan caspase inhibitor, zVAD. Ectopic expression of ATG6 suppresses cell death while reduction of ATG6 levels by siRNA sensitizes cells to TRAIL-induced cell death. Also, the inhibition of caspases leads to an increase in autophagy. These results suggest that caspase-mediated cleavage of ATG6 links the apoptotic and autophagic signaling pathways.

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