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The hsp90 family of molecular chaperones is involved in a number of signal transduction pathways, including cell division, protein folding and transport. A new member of this family was recently identified as TRAP1 (Tumor necrosis factor receptor-associated protein) or hsp75. TRAP1 is a mitochondrial protein that is an ATPase and ATP-binding protein, rendering it similar to hsp90. There is a high degree of homology between TRAP1 and hsp90 in 6 domains, however one major difference is that a highly charged domain present in hsp90 is absent in TRAP1. TRAP1 has been shown to interact with the intracellular domain of the type 1 receptor for tumor necrosis factor (TNFR-1IC) and to the retinoblastoma protein (Rb). Signaling through TNFR-1 induces antiviral responses, fibroblast proliferation, cytotoxicity, etc. TRAP1 binds TNFR-1IC outside of the death domain leading to disruption in the signaling by TNFR-1. Rb has been shown to play a pivotal role in cellular differentiation and progression through the cell cycle. TRAP1 associates with Rb via an LxCxE motif, which is common among proteins that interact with Rb through SV40 T-antigen binding domain. Thus, TRAP1 is a new member of the hsp90 family that interacts with Rb and TNFR-1IC.Immunofluorescence, Western Blotting
