Chaperoning steroid hormone signaling via reversible acetylation

Glucocorticoid receptor (GR) and related steroid hormone receptors are ligand-dependent transcription factors whose regulation is critical for both homeostasis and diseases. The structural maturation of the GR has been shown to require the Hsp90 molecular chaperone complex. Evidence indicates that H...

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Main Authors:	Kovacs, Jeffrey J., Cohen, Todd J., Yao, Tso-Pang
Format:	Online
Language:	English
Published:	The Nuclear Receptor Signaling Atlas 2005
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1402214/

id	pubmed-1402214
recordtype	oai_dc
spelling	pubmed-14022142006-04-06 Chaperoning steroid hormone signaling via reversible acetylation Kovacs, Jeffrey J. Cohen, Todd J. Yao, Tso-Pang Perspective Glucocorticoid receptor (GR) and related steroid hormone receptors are ligand-dependent transcription factors whose regulation is critical for both homeostasis and diseases. The structural maturation of the GR has been shown to require the Hsp90 molecular chaperone complex. Evidence indicates that Hsp90-dependent maturation is critical for GR ligand binding capacity and activity. While the role for Hsp90 in GR function is well established, the regulation of this process is not well understood. Here we discuss a recent finding that identifies reversible protein acetylation controlled by the deacetylase HDAC6 as a novel mechanism that regulates Hsp90-dependent GR maturation. We will also speculate on the implications of this finding in steroid hormone signaling, oncogenic transformation and its potential therapeutic utility. The Nuclear Receptor Signaling Atlas 2005-10-21 /pmc/articles/PMC1402214/ /pubmed/16604172 http://dx.doi.org/10.1621/nrs.03004 Text en Copyright © 2005, Kovacs et al. This is an open-access article distributed under the terms of the Creative Commons Non-Commercial Attribution License, which permits unrestricted non-commercial use distribution and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Kovacs, Jeffrey J. Cohen, Todd J. Yao, Tso-Pang
spellingShingle	Kovacs, Jeffrey J. Cohen, Todd J. Yao, Tso-Pang Chaperoning steroid hormone signaling via reversible acetylation
author_facet	Kovacs, Jeffrey J. Cohen, Todd J. Yao, Tso-Pang
author_sort	Kovacs, Jeffrey J.
title	Chaperoning steroid hormone signaling via reversible acetylation
title_short	Chaperoning steroid hormone signaling via reversible acetylation
title_full	Chaperoning steroid hormone signaling via reversible acetylation
title_fullStr	Chaperoning steroid hormone signaling via reversible acetylation
title_full_unstemmed	Chaperoning steroid hormone signaling via reversible acetylation
title_sort	chaperoning steroid hormone signaling via reversible acetylation
description	Glucocorticoid receptor (GR) and related steroid hormone receptors are ligand-dependent transcription factors whose regulation is critical for both homeostasis and diseases. The structural maturation of the GR has been shown to require the Hsp90 molecular chaperone complex. Evidence indicates that Hsp90-dependent maturation is critical for GR ligand binding capacity and activity. While the role for Hsp90 in GR function is well established, the regulation of this process is not well understood. Here we discuss a recent finding that identifies reversible protein acetylation controlled by the deacetylase HDAC6 as a novel mechanism that regulates Hsp90-dependent GR maturation. We will also speculate on the implications of this finding in steroid hormone signaling, oncogenic transformation and its potential therapeutic utility.
publisher	The Nuclear Receptor Signaling Atlas
publishDate	2005
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1402214/
_version_	1611381225983836160

Chaperoning steroid hormone signaling via reversible acetylation

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