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} }
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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References
SHOWING 1-10 OF 133 REFERENCES
Chaperone Function of Hsp90-Associated Proteins
- BiologyScience
- 1996
Results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells and include members of the prolyl isomerase family.
Hsp90 chaperones protein folding in vitro
- BiologyNature
- 1992
Hsp90 suppresses the formation of protein aggregates by binding to the target proteins at a stoichiometry of one Hsp90 dimer to one or two substrate molecule(s), and the yield of correctly folded and functional protein is increased significantly.
Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery*
- BiologyThe Journal of Biological Chemistry
- 1998
Hop has a novel role in the chaperone machinery as an adaptor that can integrate Hsp70 and Hsp90 interactions and is targeted for small substitutions and deletions.
In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1997
The data suggest that Hsp90 is not required for the de novo folding of most proteins, but it is required for a specific subset of proteins that have greater difficulty reaching their native conformations.
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
- BiologyEMBO reports
- 2001
A novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation is presented.
Stimulation of the weak ATPase activity of human hsp90 by a client protein.
- Biology, Computer ScienceJournal of molecular biology
- 2002
It is suggested that the rate of ATP hydrolysis is critical to the mode of action of HSp90, consistent with results that have shown that both over and under-active ATPase mutants of yeast Hsp90 have impaired function in vivo.
Molecular Chaperone Machines: Chaperone Activities of the Cyclophilin Cyp-40 and the Steroid Aporeceptor-Associated Protein p23
- BiologyScience
- 1996
In vitro folding assays showed that Cyp-40 and p23 functioned as molecular chaperones in a manner similar to that of Hsp90 or Hsp70, and both proteins interacted with the substrate to maintain a nonnative folding-competent intermediate.
Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
- BiologyNature Cell Biology
- 2001
It is reported that a screen for genes required for the immune response to bacterial endotoxins has identified a B-cell line deficient in gp96, which is compatible with cellular survival even under stress conditions and causes a defect in the formation of only a small subset of cell surface receptors.
ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
- BiologyThe EMBO journal
- 1998
This work demonstrates in vitro an inherent ATPase activity in both yeast Hsp90 and the Escherichia coli homologue HtpG, which is sensitive to inhibition by the Hsp 90‐specific antibiotic geldanamycin, and suggests an ATP‐coupled chaperone cycle for HSp90‐mediated protein folding.