| First Author | Han J | Year | 2014 |
| Journal | J Biol Chem | Volume | 289 |
| Issue | 10 | Pages | 6485-97 |
| PubMed ID | 24362031 | Mgi Jnum | J:213031 |
| Mgi Id | MGI:5582706 | Doi | 10.1074/jbc.M113.536854 |
| Citation | Han J, et al. (2014) A Complex between Atg7 and Caspase-9: A NOVEL MECHANISM OF CROSS-REGULATION BETWEEN AUTOPHAGY AND APOPTOSIS. J Biol Chem 289(10):6485-97 |
| abstractText | 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. |
