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
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.
Cellular Processing of the Glucocorticoid Receptor Gene and Protein: New Mechanisms for Generating Tissue-specific Actions of Glucocorticoids*
TLDR
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
The Glucocorticoid Receptor
TLDR
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.
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.
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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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.
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TLDR
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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.
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