In Vitro Inhibitory Mechanism Effect of TRAIP on the Function of TRAF2 Revealed by Characterization of Interaction Domains.
TRAF-interacting protein (TRAIP), a negative regulator of TNF-induced-nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) 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-κB 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-κB signaling.
Mesh Terms:
Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Maps, Protein Multimerization, Protein Stability, TNF Receptor-Associated Factor 2, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
Humans, Protein Binding, Protein Interaction Domains and Motifs, Protein Interaction Maps, Protein Multimerization, Protein Stability, TNF Receptor-Associated Factor 2, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
Int J Mol Sci
Date: Aug. 20, 2018
PubMed ID: 30127245
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