Cited by 774Heat shock proteins researchHistone Deacetylase Inhibitors ResearchUbiquitin and proteasome pathways

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Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90

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Bali, Purva, Pranpat, Michael, Bradner, James, Balasis, Maria, Fiskus, Warren, Guo, Fei, Rocha, Kathy, Kumaraswamy, Sandhya, Boyapalle, Sandhya, Atadja, Peter, Seto, Edward, Bhalla, Kapil·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.c500186200

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Abstract

The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90. This promotes the polyubiquitylation and degradation of the pro-growth and pro-survival client proteins Bcr-Abl, mutant FLT-3, c-Raf, and AKT in human leukemia cells. HDAC6 is a member of the class IIB HDACs. It is predominantly cytosolic, microtubule-associated alpha-tubulin deacetylase that is also known to promote aggresome inclusion of the misfolded polyubiquitylated proteins. Here we demonstrate that in the Bcr-abl oncogene expressing human leukemia K562 cells, HDAC6 can be co-immunoprecipitated with HSP90, and the knock-down of HDAC6 by its siRNA induced the acetylation of HSP90 and alpha-tubulin. Depletion of HDAC6 levels also inhibited the binding of HSP90 to ATP, reduced the chaperone association of HSP90 with its client proteins, e.g. Bcr-Abl, and induced polyubiquitylation and partial depletion of Bcr-Abl. Conversely, the ectopic overexpression of HDAC6 inhibited LAQ824-induced acetylation of HSP90 and alpha-tubulin and reduced LAQ824-mediated depletion of Bcr-Abl, AKT, and c-Raf. Collectively, these findings indicate that HDAC6 is also an HSP90 deacetylase. Targeted inhibition of HDAC6 leads to acetylation of HSP90 and disruption of its chaperone function, resulting in polyubiquitylation and depletion of pro-growth and pro-survival HSP90 client proteins including Bcr-Abl. Depletion of HDAC6 sensitized human leukemia cells to HAA-HDIs and proteasome inhibitors.

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Authors: Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., Seto, E., & Bhalla, K.
Affiliations: Moffitt Cancer Center (US)
Dana-Farber Cancer Institute (US)
Novartis (United States) (US)
Corresponding author: Bhalla, Kapil
ORCID: Bradner, James
Balasis, Maria
Fiskus, Warren
Guo, Fei
Seto, Edward
Bhalla, Kapil
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-07
Volume: 280
Issue: 29
Pages: 26729-26734
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.c500186200
OpenAlex: W2151445954
Cited by: 755
References: 42
Citations by year: 2026: 9 · 2025: 16 · 2024: 10 · 2023: 9 · 2022: 23 · 2021: 21 · 2020: 38 · 2019: 33 · 2018: 32 · 2017: 28 · 2016: 34 · 2015: 40 · 2014: 45 · 2013: 42 · 2012: 47
FWCI: 19.90
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5555 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
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, LAQ824, panobinostat, BCR-ABL, alpha-tubulin deacetylation, polyubiquitination, Hsp90 client proteins, Akt, Raf-1, leukemia, K562 cells, proteasome inhibitors, siRNA knockdown
MeSH terms: Histone Deacetylase 6, Panobinostat, Acetylation, Antineoplastic Agents, Enzyme Inhibitors, Histone Deacetylases, Humans, Hydroxamic Acids, Indoles, Leukemia, Neoplasm Proteins, Protein Binding, Molecular Chaperones, HSP90 Heat-Shock Proteins, K562 Cells, Ubiquitin, Histone Deacetylase Inhibitors

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Inhibition of Histone Deacetylase 6 Acetylates and Disrupts the Chaperone Function of Heat Shock Protein 90

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