The glucocorticoid responses are shaped by molecular chaperones

@article{Grad2007TheGR,
  title={The glucocorticoid responses are shaped by molecular chaperones},
  author={Iwona Grad and Didier Picard},
  journal={Molecular and Cellular Endocrinology},
  year={2007},
  volume={275},
  pages={2-12}
}
  • I. Grad, D. Picard
  • Published 15 September 2007
  • Biology
  • Molecular and Cellular Endocrinology
View on Elsevier
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370 Citations
Highly Influential Citations
21
Background Citations
171
Methods Citations
4
Results Citations
2

370 Citations

Citation Type

Citation Type

40 – Nuclear Mechanisms of Glucocorticoid Action
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The origin and molecular properties of the GR isoforms and their contribution to the sensitivity and specificity of the glucocorticoid response are discussed.
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The molecular and cellular mechanisms of GR signaling, and the potential role for GR isoforms in regulating the specificity and sensitivity of glucocorticoid responsiveness in healthy and diseased tissues are discussed.
SUMO conjugation as regulator of the glucocorticoid receptor-FKBP51 cellular response to stress
Hsp90-Mediated Maturation of Kinases andNuclear Steroid Hormone Receptors:A Dissertation
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It is found that ATP binding and hydrolysis by Hsp90 are both required for the efficient maturation of the glucocorticoid hormone receptor (GR) and vsrc confirming the critical role of ATPHydrolysis in the m maturity of steroid hormone receptors and kinases in vivo.
Role of molecular chaperones and TPR-domain proteins in the cytoplasmic transport of steroid receptors and their passage through the nuclear pore
TLDR
Experimental evidence is consistent with a model where the chaperone machinery is required for the retrotransport of the receptor through the cytoplasm and also facilitates the passage through the nuclear pore.
From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery.
TLDR
This review considers specialized functions of the Hsp70 chaperone machinery mediated by its cochaperones and focuses on vesicular trafficking, protein degradation and a potential role in G protein-coupled receptor processing.
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References

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In this review, the functions of molecular chaperones during steroid receptor maturation are explored, leading to a general mechanistic model indicative of chaperone cooperation in protein folding.
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TLDR
The initial GR interaction with hsp70 appears to be critical for the triage between hsp90 heterocomplex assembly and preservation of receptor function vs CHIP-dependent ubiquitylation and proteasomal degradation.
Chaperoning steroid hormone action
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  • Biology
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The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.
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A novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation is presented.
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Immunofluorescence and fractionation revealed hormone-induced translocation of the hormone-generated GR·Hsp90·FKBP52·dynein complex from cytoplasm to nucleus, a step that precedes dissociation of the complex within the nucleus and conversion of GR to the DNA-binding form.
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TLDR
This work shows that addition of p23 to native GR·hsp90 heterocomplexes immunoadsorbed from L cell cytosol or toGR·hSp90 hetercomplexes prepared with the minimal assembly system inhibits both receptor heterocom Complex disassembly and loss of steroid binding activity.
Inhibition of GR‐mediated transcription by p23 requires interaction with Hsp90
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