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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368 Citations
Highly Influential Citations
21
Background Citations
170
Methods Citations
4
Results Citations
2

368 Citations

Citation Type

Citation Type

40 – Nuclear Mechanisms of Glucocorticoid Action
The FKBP51 Glucocorticoid Receptor Co-Chaperone: Regulation, Function, and Implications in Health and Disease
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An update on the role of the different co-chaperones of Hsp70 and Hsp90 in the regulation of GR function is provided and the evidence portraying FKBP51 as a scaffolding protein organizing protein complexes rather than a chaperone contributing to the folding of individual proteins is collated.
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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.
Modulation of the Glucocorticoid Receptor Activity by Post-Translational Modifications
Glucocorticoids (GCs) regulate numerous physiologic processes in order to maintain homeostasis. Most of their actions are mediated by an intracellular GC receptor (GR). The dysregulation of the GR…
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The Glucocorticoid Receptor
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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
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.
Hsp90-Mediated Maturation of Kinases andNuclear Steroid Hormone Receptors:A Dissertation
TLDR
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.
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

SHOWING 1-10 OF 102 REFERENCES
Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteins
TLDR
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.
Chaperoning of glucocorticoid receptors.
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
  • D. Picard
  • Biology
    Trends in Endocrinology & Metabolism
  • 2006
The molecular chaperone Hsp90 can negatively regulate the activity of a glucocorticosteroid-dependent promoter.
  • K. Kang, X. Meng, M. Catelli
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
It is proposed that an increased Hsp90/GR ratio influences the responsiveness to ligand at a step that is after receptor activation, and this increased ratio may be of pathophysiological relevance in the different circumstances that lead to an elevated level of nuclear HSp90.
From the cradle to the grave: molecular chaperones that may choose between folding and degradation
TLDR
A novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation is presented.
HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor.
A New First Step in Activation of Steroid Receptors
TLDR
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.
Heat-shock protein 90, a chaperone for folding and regulation
  • D. Picard
  • Biology
    Cellular and Molecular Life Sciences CMLS
  • 2002
TLDR
The large conformational flexibility of HSp90 and a multitude of dynamic co-chaperone complexes contribute to generating functional diversity, and allow Hsp90 to assist a wide range of substrates.
Folding of the Glucocorticoid Receptor by the Heat Shock Protein (hsp) 90-based Chaperone Machinery
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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