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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

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.

Y. Choi, is an assistant investigator of the Howard Hughes Medical Institute.

¹Abbreviations used in this paper: β-gal; β-galactosidase; c-IAP, cellular inhibitors of apoptosis protein; GST, glutathione-S-transferase; h, human; IL-1R, IL-1 receptor; m, mouse; TNFR, TNF receptor; TRAF, TNFRassociated factor; TRIP, TRAF-interacting protein.

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