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Updated: Jul 6, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
Published on: September 21, 2011
Yeast molecular chaperones and the mechanism of steroid hormone action
1Department of Cell Biology and Anatomy, Mount Sinai Medical Center, New York, NY 10029, USA.
Abstract:
The yeast Saccharomyces cerevisiae has become a valuable tool for the analysis of steroid action in vivo. Results from studies using yeast have been productive for understanding the role of molecular chaperones, especially Hsp90 and its cochaperones, in regulating the activation of heterologously expressed steroid hormone receptors. The methodology for these investigations involves assaying receptor function in yeast strains with deletions or mutations in the genes encoding molecular chaperone proteins. The information obtained thus far indicates that the Hsp90 chaperone machine functions in vivo to maintain steroid receptors in a high-affinity hormone-binding conformation and also in downstream events of the activation pathway.
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