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.