Molecular Cloning of TNF Receptor-Associated Factor (TRAF) 1-Binding Protein

Abstract

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 utilized the yeast two-hybrid system to clone cDNAs encoding proteins that bind to a TRAF domain of TRAF1. A cDNA encoding a putative signal transducer, designated T1BP (TRAF1-binding protein), has been moleculary cloned. T1BP specifically interacts with TRAF1 through its interaction with the TRAF domain, but failed to interact with TRAF2. When overexpressed, T1BP associates with the CD30 or TNFR2 signaling complex through its interaction with TRAF1. Moreover, we demonstrate that T1BP inhibits an antiapoptotic effect of TRAF1. Thus, T1BP may influence signals responsible for cell survival induced by TRAF1.