| First Author | Lee SY | Year | 1997 |
| Journal | J Exp Med | Volume | 185 |
| Issue | 7 | Pages | 1275-85 |
| PubMed ID | 9104814 | Mgi Jnum | J:39510 |
| Mgi Id | MGI:86904 | Doi | 10.1084/jem.185.7.1275 |
| Citation | Lee SY, et al. (1997) 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. J Exp Med 185(7):1275-85 |
| abstractText | 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. |
