Heat-shock protein 90, a chaperone for folding and regulation |
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Authors: | Picard D |
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Institution: | (1) 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, CH |
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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. |
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Keywords: | , Molecular chaperone, protein folding, p23, Hop, Cdc37, immunophilins, |
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