J. Exp. Med.
© The Rockefeller University Press
0022-1007/97/04/1275/12 $2.00
Volume 185, Number 7, April 7, 1997 1275-1286

TRAF-interacting Protein (TRIP): A Novel Component of the Tumor Necrosis Factor Receptor (TNFR)- and CD30-TRAF Signaling Complexes That Inhibits TRAF2-mediated NF-B Activation

By Soo Young Lee, Sang Yull Lee,^* and Yongwon Choi^*

From the ^* Howard Hughes Medical Institute, New York 10021; and  The Rockefeller University, New York 10021

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-B 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.

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