TRAF-interacting protein (TRIP): a novel component of the tumor necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes that inhibits TRAF2-mediated NF-kappaB activation.

Through their interaction with the TNF receptor-associated factor (TRAF) family, members of the tumor necrosis factor receptor (TNFR) superfamily elicit a wide range of biological effects including differentiation, proliferation, activation, or cell death. We have identified and characterized a novel component of the receptor-TRAF signaling complex, designated TRIP (TRAF-interacting protein), ...
which contains a RING finger motif and an extended coiled-coil domain. TRIP associates with the TNFR2 or CD30 signaling complex through its interaction with TRAF proteins. When associated, TRIP inhibits the TRAF2-mediated NF-kappaB activation that is required for cell activation and also for protection against apoptosis. Thus, TRIP acts as a receptor-proximal regulator that may influence signals responsible for cell activation/proliferation and cell death induced by members of the TNFR superfamily.
Mesh Terms:
Amino Acid Sequence, Antigens, CD30, Base Sequence, Binding Sites, Cloning, Molecular, Gene Expression Regulation, Developmental, Models, Biological, Molecular Sequence Data, NF-kappa B, Protein Binding, Protein Structure, Secondary, Proteins, Receptors, Tumor Necrosis Factor, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Signal Transduction, TNF Receptor-Associated Factor 1, TNF Receptor-Associated Factor 2, Tissue Distribution, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
J. Exp. Med.
Date: Apr. 07, 1997
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