Heat-shock protein 90, a chaperone for folding and regulation
Copyright policy )Heat-shock protein 90, a chaperone for folding and regulation
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.
- University of Geneva Switzerland
570, Protein Folding, Molecular Chaperones/metabolism, Binding Sites, Signal Transduction/physiology, Cell Cycle, Substrate Specificity, HSP90 Heat-Shock Proteins/chemistry/metabolism, Animals, Humans, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Cell Cycle/physiology, Molecular Chaperones, Signal Transduction, ddc: ddc:570
570, Protein Folding, Molecular Chaperones/metabolism, Binding Sites, Signal Transduction/physiology, Cell Cycle, Substrate Specificity, HSP90 Heat-Shock Proteins/chemistry/metabolism, Animals, Humans, Amino Acid Sequence, HSP90 Heat-Shock Proteins, Cell Cycle/physiology, Molecular Chaperones, Signal Transduction, ddc: ddc:570
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