Anatomy of TRAF2. Distinct domains for nuclear factor- Kappa B activation and association with tumor necrosis factor signaling proteins

The tumor necrosis factor (TNF) receptor-associated factor (TRAF) family of proteins interact with and transduce signals for members of the TNF receptor superfamily. TRAF1, TRAF2, and TRAF3 share a conserved C-terminal TRAF domain. TRAF2 plays a key role in transducing signals for activation of the...

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Veröffentlicht in:The Journal of biological chemistry 1996, Vol.271 (33), p.19935-19942
Hauptverfasser: Takeuchi, M, Rothe, M, Goeddel, D V
Format: Artikel
Sprache:eng
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Zusammenfassung:The tumor necrosis factor (TNF) receptor-associated factor (TRAF) family of proteins interact with and transduce signals for members of the TNF receptor superfamily. TRAF1, TRAF2, and TRAF3 share a conserved C-terminal TRAF domain. TRAF2 plays a key role in transducing signals for activation of the transcription factor nuclear factor- Kappa B (NF- Kappa B). We have performed extensive mutational analysis on TRAF2, examining the requirements for NF- Kappa B activation, self-association, and interaction with other molecules involved in TNF signaling. Examination of point mutants and TRAF2-TRAF3 chimeric proteins indicates that the N-terminal RING finger and two adjacent zinc fingers of TRAF2 are required for NF- Kappa B activation. The two distinct TRAF-N and TRAF-C subdomains of the TRAF domain appear to independently mediate self-association and interaction with TRAF1. Interaction of TRAF2 with TNF-R2 and TRADD requires sequences at the C terminus of the TRAF-C domain, whereas interaction with the protein kinase receptor-interacting protein V(RIP) occurs via sequences at the N terminus of the TRAF-C domain. Thus, distinct domains of TRAF2 are involved in recruitment and signaling functions.
ISSN:0021-9258
DOI:10.1074/jbc.271.33.19935