| First Author | Lamkanfi M | Year | 2005 |
| Journal | J Biol Chem | Volume | 280 |
| Issue | 8 | Pages | 6923-32 |
| PubMed ID | 15590671 | Mgi Jnum | J:97069 |
| Mgi Id | MGI:3574225 | Doi | 10.1074/jbc.M411180200 |
| Citation | Lamkanfi M, et al. (2005) A novel caspase-2 complex containing TRAF2 and RIP1. J Biol Chem 280(8):6923-32 |
| abstractText | The enzymatic activity of caspases is implicated in the execution of apoptosis and inflammation. Here we demonstrate a novel nonenzymatic function for caspase-2 other than its reported proteolytic role in apoptosis. Caspase-2, unlike caspase-3, -6, -7, -9, -11, -12, and -14, is a potent inducer of NF-kappaB and p38 MAPK activation in a TRAF2-mediated way. Caspase-2 interacts with TRAF1, TRAF2, and RIP1. Furthermore, we demonstrate that endogenous caspase-2 is recruited into a large and inducible protein complex, together with TRAF2 and RIP1. Structure-function analysis shows that NF-kappaB activation occurs independent of enzymatic activity of the protease and that the caspase recruitment domain of caspase-2 is sufficient for the activation of NF-kappaB and p38 MAPK. These results demonstrate the inducible assembly of a novel protein complex consisting of caspase-2, TRAF2, and RIP1 that activates NF-kappaB and p38 MAPK through the caspase recruitment domain of caspase-2 independently of its proteolytic activity. |
