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Song, HY, Dunbar, JD, Zhang, YX, Guo, D and Donner, DB (1995) Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 270:3574-81


The yeast-based two hybrid has been used to identify a novel protein that binds to the intracellular domain of the type 1 receptor for tumor necrosis factor (TNFR-1IC). The TNF receptor-associated protein, TRAP-1, shows strong homology to members of the 90-kDa family of heat shock proteins. After in vitro transcription/translation and 35S labeling, TRAP-1 was precipitated using a fusion protein consisting of glutathione S-transferase and TNFR-1IC, showing that the two proteins directly interact. The ability of deletion mutants of TNFR-1 to interact with TRAP-1 was tested using the two hybrid system. This showed that the amino acid sequences that mediate binding are diffusely distributed outside of the domain in the C terminus of TNFR-1IC that signals cytotoxicity. The 2.4-kilobase TRAP-1 mRNA was variably expressed in skeletal muscle, liver, heart, brain, kidney, pancreas, lung, and placenta. TRAP-1 mRNA was also detected in each of eight different transformed cell lines. Identification of TRAP-1 may be an important step toward defining how TNFR-1, which does not contain protein tyrosine kinase activity, transmits its message to signal transduction pathways.




Amino Acid Sequence; Animals; Base Sequence; DNA, Complementary; HSP90 Heat-Shock Proteins/genetics; HSP90 Heat-Shock Proteins/metabolism; HeLa Cells; Humans; Molecular Sequence Data; Protein Binding; Rats; Receptors, Tumor Necrosis Factor/metabolism; Sequence Homology, Amino Acid; Signal Transduction



Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status



GO:0005164: tumor necrosis factor receptor binding

ECO:0000303: author statement without traceable support used in manual assertion


Seeded From UniProt


See also


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