Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles

@article{Kirschke2014GlucocorticoidRF,
  title={Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles},
  author={Elaine Kirschke and Devrishi Goswami and Daniel R Southworth and Patrick R. Griffin and David A. Agard},
  journal={Cell},
  year={2014},
  volume={157},
  pages={1685-1697}
}
The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90 molecular chaperone for in vivo function. Although Hsp90 is required for ligand binding in vivo, purified apo GR is capable of binding ligand with no enhancement from Hsp90. We reveal that Hsp70, known to facilitate client delivery to Hsp90, inactivates GR through partial unfolding, whereas Hsp90 reverses this inactivation. Full recovery of ligand binding requires ATP hydrolysis on Hsp90 and the Hop and p23… CONTINUE READING
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