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

@article{Picard2002HeatshockP9,
  title={Heat-shock protein 90, a chaperone for folding and regulation},
  author={Didier Picard},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2002},
  volume={59},
  pages={1640-1648}
}
  • D. Picard
  • Published 1 October 2002
  • Biology
  • Cellular and Molecular Life Sciences CMLS
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… 
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TLDR
The current knowledge on the functional principles of this molecular machine, including the ATPdriven chaperone cycle of Hsp90 and its regulation by co-chaperones and post-translational modifications are summarized.
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This review, looks at the many different levels by which Hsp90 activity is ultimately regulated and some are directly responsible for delivery of client protein.
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This review summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction.
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