Cited by 1,153Heat shock proteins researchHistone Deacetylase Inhibitors ResearchUbiquitin and proteasome pathways

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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

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Kovacs, Jeffrey J., Murphy, Patrick J.M., Gaillard, Stéphanie, Zhao, Xuan, Wu, June-Tai, Nicchitta, Christopher V., Yoshida, Minoru, Toft, David O., Pratt, William B., Yao, Tso-Pang·2005·Molecular Cell

DOI 10.1016/j.molcel.2005.04.021

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Abstract

The molecular chaperone heat shock protein 90 (Hsp90) and its accessory cochaperones function by facilitating the structural maturation and complex assembly of client proteins, including steroid hormone receptors and selected kinases. By promoting the activity and stability of these signaling proteins, Hsp90 has emerged as a critical modulator in cell signaling. Here, we present evidence that Hsp90 chaperone activity is regulated by reversible acetylation and controlled by the deacetylase HDAC6. We show that HDAC6 functions as an Hsp90 deacetylase. Inactivation of HDAC6 leads to Hsp90 hyperacetylation, its dissociation from an essential cochaperone, p23, and a loss of chaperone activity. In HDAC6-deficient cells, Hsp90-dependent maturation of the glucocorticoid receptor (GR) is compromised, resulting in GR defective in ligand binding, nuclear translocation, and transcriptional activation. Our results identify Hsp90 as a target of HDAC6 and suggest reversible acetylation as a unique mechanism that regulates Hsp90 chaperone complex activity.

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Authors: Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P.
Affiliations: Duke University (US)
University of Michigan (US)
Japan Science and Technology Agency (JP)
Mayo Clinic (US)
Corresponding author: Yao, Tso-Pang
ORCID: Kovacs, Jeffrey J.
Zhao, Xuan
Wu, June-Tai
Nicchitta, Christopher V.
Yoshida, Minoru
Yao, Tso-Pang
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2005-05
Volume: 18
Issue: 5
Pages: 601-607
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2005.04.021
OpenAlex: W1990011854
Cited by: 1,153
References: 25
Citations by year: 2026: 39 · 2025: 49 · 2024: 44 · 2023: 37 · 2022: 55 · 2021: 48 · 2020: 51 · 2019: 50 · 2018: 49 · 2017: 47 · 2016: 63 · 2015: 69 · 2014: 71 · 2013: 69 · 2012: 59
FWCI: 20.58
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 3035 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: Leukemia and Lymphoma Society
American Cancer Society (RSG-03-147-01-CSM)
National Institutes of Health (DK31573, CA28010)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: HDAC6, HSP90, HSP90 acetylation, glucocorticoid receptor, p23, steroid hormone receptors, nuclear translocation, transcriptional activation, ligand binding
MeSH terms: Histone Deacetylase 6, Acetylation, Animals, Cell Line, Dexamethasone, Glucocorticoids, Histone Deacetylases, Humans, Receptors, Glucocorticoid, Transcription, Genetic, Signal Transduction, HSP90 Heat-Shock Proteins, Mice

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HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor

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