Cellular and Molecular Life Sciences CMLS

, Volume 59, Issue 10, pp 1640–1648

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

Authors

  • D. Picard
    • Département de Biologie Cellulaire, Université de Genève, Sciences III, 30 quai Ernest-Ansermet, 1211 Genève 4 (Switzerland), Fax +41 22 702 6928, e-mail: Picard@cellbio.unige.ch

DOI: 10.1007/PL00012491

Cite this article as:
Picard, D. CMLS, Cell. Mol. Life Sci. (2002) 59: 1640. doi:10.1007/PL00012491

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.

Key words. Molecular chaperone; protein folding; p23; Hop; Cdc37; immunophilins.

Copyright information

© Birkhäuser Verlag, 2002