title: Heat-shock protein 90, a chaperone for folding and regulation.
abstract: Heat-shock protein 90 (Hsp90) is an abundant and highly conserved molecular chaperone that is essential for viability in eukaryotes. Hsp90 fulfills a housekeeping function in contributing to the folding, maintenance of structural integrity and proper regulation of a subset of cytosolic proteins. A remarkable proportion of its substrates are proteins involved in cell cycle control and signal transduction. Hsp90 acts with a cohort of Hsp90 co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. The large conformational flexibility of Hsp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.
authors.affiliation: Picard@cellbio.unige.ch
authors.forename: D
authors.initials: D
authors.lastname: Picard
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002453:Cell Cycle / Q000502:physiology; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D015398:Signal Transduction / Q000502:physiology; D013379:Substrate Specificity
chemical_list: D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones