title: TRAP-1, the mitochondrial Hsp90.
abstract: Protein folding quality control does not occur randomly in cells, but requires the action of specialized molecular chaperones compartmentalized in subcellular microenvironments and organelles. Fresh experimental evidence has now linked a mitochondrial-specific Heat Shock Protein-90 (Hsp90) homolog, Tumor Necrosis Factor Receptor-Associated Protein-1 (TRAP-1) to pleiotropic signaling circuitries of organelle integrity and cellular homeostasis. TRAP-1-directed compartmentalized protein folding is broadly exploited in cancer and neurodegenerative diseases, presenting new opportunities for therapeutic intervention in humans. This article is part of a Special Issue entitled: Heat Shock Protein 90 (Hsp90).
authors: Prostate Cancer Discovery and Development Program, USA. daltieri@wistar.org
authors: Dario C
authors: DC
authors: Altieri
authors: Gary S
authors: GS
authors: Stein
authors: Jane B
authors: JB
authors: Lian
authors: Lucia R
authors: LR
authors: Languino
mesh_terms: D060833:Cellular Microenvironment / Q000502:physiology; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones; C092306:TRAP1 protein, human