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J Biol Chem. 2014 Mar 7;289(10):6485-97. doi: 10.1074/jbc.M113.536854. Epub 2013 Dec 20.

A Complex between Atg7 and Caspase-9: A NOVEL MECHANISM OF CROSS-REGULATION BETWEEN AUTOPHAGY AND APOPTOSIS.

Author information

1
From the Departments of Pathology and.

Abstract

Several cross-talk mechanisms between autophagy and apoptosis have been identified, in which certain co-regulators are shared, allowing the same protein to participate in these opposing processes. Our studies suggest that caspase-9 is a novel co-regulator of apoptosis and autophagy and that its caspase catalytic activity is dispensable for its autophagic role. We provide evidence that caspase-9 facilitates the early events leading to autophagosome formation; that it forms a complex with Atg7; that Atg7 is not a direct substrate for caspase-9 proteolytic activity; and that, depending on the cellular context, Atg7 represses the apoptotic capability of caspase-9, whereas the latter enhances the Atg7-mediated formation of light chain 3-II. The repression of caspase-9 apoptotic activity is mediated by its direct interaction with Atg7, and it is not related to the autophagic function of Atg7. We propose that the Atg7·caspase-9 complex performs a dual function of linking caspase-9 to the autophagic process while keeping in check its apoptotic activity.

KEYWORDS:

Apoptosis; Autophagy; Caspase; Cell Death; Cellular Regulation

PMID:
24362031
PMCID:
PMC3945314
DOI:
10.1074/jbc.M113.536854
[Indexed for MEDLINE]
Free PMC Article
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