| Literature DB >> 8548810 |
M Rothe1, M G Pan, W J Henzel, T M Ayres, D V Goeddel.
Abstract
The 75 kDa tumor necrosis factor receptor (TNFR2) transduces extracellular signals via receptor-associated cytoplasmic proteins. Two of these signal transducers, TRAF1 and TRAF2, were isolated and characterized previously. We report here the biochemical purification and subsequent molecular cloning of two novel TNFR2-associated proteins, designated c-IAP1 and c-IAP2, that are closely related mammalian members of the inhibitor of apoptosis protein (IAP) family originally identified in baculoviruses. The viral and cellular IAPs contain N-terminal baculovirus IAP repeat (BIR) motifs and a C-terminal RING finger. The c-IAPs do not directly contact TNFR2, but rather associate with TRAF1 and TRAF2 through their N-terminal BIR motif-comprising domain. The recruitment of c-IAP1 or c-IAP2 to the TNFR2 signaling complex requires a TRAF2-TRAF1 heterocomplex.Entities:
Mesh：
Substances：
Year: 1995 PMID： 8548810 DOI： 10.1016/0092-8674(95)90149-3
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582