The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins
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.
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XIAP inhibits TNF-α-induced cell death and its expression is regulated by NF-κB.
“XIAP inhibits TNF-α-induced cell death and its expression is regulated by NF-κB (Chu et al., 1997; Rothe et al., 1995; Stehlik et al., 1998).”
From Evidence for miR‐181 involvement in neuroinflammatory responses of astrocytes (2013) · cites this paper as Rothe et al., 1995
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- Authors
- Rothe, M., Pan, M.-G., Henzel, W. J., Ayres, T. M., & V. Goeddel, D.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 83
- Issue
- 7
- Pages
- 1243-1252
- ISSN
- 0092-8674
- Cited by
- 1,030
- References
- 1
- Language
- en
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