Scientific article

Heat-shock protein 90, a chaperone for folding and regulation

ContributorsPicard, Didierorcid
Published inCellular and molecular life sciences, vol. 59, no. 10, p. 1640-1648
Publication date2002

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.

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Cycle/physiology
  • HSP90 Heat-Shock Proteins/chemistry/metabolism
  • Humans
  • Molecular Chaperones/metabolism
  • Protein Folding
  • Signal Transduction/physiology
  • Substrate Specificity
Citation (ISO format)
PICARD, Didier. Heat-shock protein 90, a chaperone for folding and regulation. In: Cellular and molecular life sciences, 2002, vol. 59, n° 10, p. 1640–1648.
Main files (1)
Article (Published version)
ISSN of the journal1420-682X

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