Heat-shock protein 90, a chaperone for folding and regulation
D Picard - Cellular and Molecular Life Sciences CMLS, 2002 - Springer
D Picard
Cellular and Molecular Life Sciences CMLS, 2002•SpringerHeat-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 …
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 …
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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