| First Author | McCarthy JV | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 27 | Pages | 16968-75 |
| PubMed ID | 9642260 | Mgi Jnum | J:48493 |
| Mgi Id | MGI:1270063 | Doi | 10.1074/jbc.273.27.16968 |
| Citation | McCarthy JV, et al. (1998) RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase. J Biol Chem 273(27):16968-75 |
| abstractText | Through specific interactions with members of the tumor necrosis receptor (TNFR) family, adapter molecules such as the serine/threonine (Ser/Thr) kinase RIP mediate divergent signaling pathways including NF-kappaB activation and cell death. In this study, we have identified and characterized a novel 61-kDa protein kinase related to RIP that is a component of both the TNFR-1 and the CD40 signaling complexes. Receptor interacting protein-2 (RIP2) contains an N-terminal domain with homology to Ser/Thr kinases and a C-terminal caspase activation and recruitment domain (CARD), a homophilic interaction motif that mediates the recruitment of caspase death proteases. Overexpression of RIP2 signaled both NF-kappaB activation and cell death. Mutational analysis revealed the pro-apoptotic function of RIP2 to be restricted to its C-terminal CARD domain, whereas the intact molecule was necessary for NF-kappaB activation. RIP2 interacted with other members of the TNFR-1 signaling complex, including inhibitor of apoptosis protein cIAP1 and with members of the TNFR-associated factor (TRAF) family, specifically TRAF1, TRAF5, and TRAF6, but not with TRAF2, TRAF3, or TRAF4. These TRAF interactions mediate the recruitment of RIP2 to receptor signaling complexes. |
