In Vitro Inhibitory Mechanism Effect of TRAIP on the Function of TRAF2 Revealed by Characterization of Interaction Domains
- Authors
- Bhat, Eijaz Ahmed; Kim, Chang Min; Kim, Sunghwan; Park, Hyun Ho
- Issue Date
- Aug-2018
- Publisher
- MDPI
- Keywords
- immune response; nuclear factor-kappa B; tumor necrosis factor-receptor associated factor; TRAF-interacting protein; protein interaction
- Citation
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.19, no.8
- Journal Title
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Volume
- 19
- Number
- 8
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/1938
- DOI
- 10.3390/ijms19082457
- ISSN
- 1422-0067
1422-0067
- Abstract
- TRAF-interacting protein (TRAIP), a negative regulator of TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-kappa B) activation, inhibits adaptor protein TRAF2 by direct interaction and is critical in apoptosis, cell proliferation, antiviral response, and embryonic development. Although the critical function of TRAIP in NF-kappa B signaling is well-known, the molecular inhibitory mechanism of TRAIP remains unclear. We found that the TRAIP coiled-coil domain altered its stoichiometry between dimer and trimer in a concentration-dependent manner. Additionally, the TRAIP RING domain induced even higher-ordered assembly, which was necessary for interacting with the TRAF-N domain of TRAF2 but not TRAF1. Characterization of the TRAF-N domains of TRAF1 and TRAF2, the tentative TRAIP-binding region of TRAFs, suggested the molecular basis of the inhibitory effect of TRAIP on TRAF2 in NF-kappa B signaling.
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