| Literature DB >> 21878357 |
Dario C Altieri1, Gary S Stein, Jane B Lian, Lucia R Languino.
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). Copyright ÂEntities:
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Year: 2011 PMID: 21878357 PMCID: PMC3263322 DOI: 10.1016/j.bbamcr.2011.08.007
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002