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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination
Abstract
Histone deacetylase 6 (HDAC6) is a unique enzyme with specific structural and functional features. It is actively or stably maintained in the cytoplasm and is the only member, within the histone deacetylase family, that harbors a full duplication of its deacetylase homology region followed by a specific ubiquitin-binding domain at the C-terminus end. Accordingly, this deacetylase functions at the heart of a cellular regulatory mechanism capable of coordinating various cellular functions largely relying on the microtubule network. Moreover, HDAC6 action as a regulator of the HSP90 chaperone activity adds to the multifunctionality of the protein, and allows us to propose a critical role for HDAC6 in mediating and coordinating various cellular events in response to different stressful stimuli.
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“HDAC6 has recently emerged as an attractive target for the treatment of cancer (Boyault et al, 2007; Lee et al, 2008; Kawada et al, 2009; Rivieccio et al, 2009).”
From A novel small molecule hydroxamate preferentially inhibits HDAC6 activity and tumour growth (2013) · cites this paper as Boyault et al, 2007
In the citing paper
“HDAC6 has emerged as an attractive target for drug development and research.11,12”
From Rational Design and Simple Chemistry Yield a Superior, Neuroprotective HDAC6 Inhibitor, Tubastatin A (2010) · cites this paper as [12]
In the citing paper
“HDAC6 seems to be very sensitive to PROTAC-mediated degradation, probably because of its dominant cytoplasmic localization, whereas most other isoforms are localized in the nucleus [139].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [139]
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Self-citationTubulin modifications and their cellular functions
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Histone deacetylase 6 interacts with the microtubule‐associated protein tau
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“This review will discuss the role of HDAC6 in the pathogenesis and treatment of cancer.”
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“The acetyl-K40-mediated tubulin degradation could involve HDAC6, because this protein binds to acetyl-K40 -tubulin and interacts with proteins that mediate ubiquitylation (Boyault et al., 2007).”
BackgroundHDAC6 as privileged target in drug discovery: A perspective
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The Cytoplasmic Deacetylase HDAC6 Is Required for Efficient Oncogenic Tumorigenesis
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Regulation of microtubule dynamics by inhibition of the tubulin deacetylase HDAC6
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“These include histone deacetylase 6 (HDAC6), a member of the class II histone deacetylases (Boyault et al., 2007a; Hubbert et al., 2002; Matsuyama et al., 2002; Zhang et al., 2003), and SIRT2, a class III NAD-dependent histone deacetylase (North et al., 2003).”
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“HDAC6 is an unusual deacetylase characterized by cyto- plasmic localization, ubiquitin-binding capacity, and impact on tubulin and actin cytoskeleton (Boyault et al, 2007a).”
BackgroundRole of Acetylation and Extracellular Location of Heat Shock Protein 90α in Tumor Cell Invasion
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“Although it is likely that not all of the known hsp90 client proteins would be uniformly affected (38), posttranslational modifications of hsp90 such as phosphorylation and acetylation influence the chaperone function of hsp90, thereby affecting the signaling networks that govern the malignant phenotype and response t…”
BackgroundHUANG, S. H., Wang, S., Bian, C., Yang, Z., Zhou, H., Zeng, Y. C., Li, H., Han, Q., & Zhao, R. C. (2012) · Stem Cells and Development · doi:10.1089/scd.2012.0014 · Cited by 216
“Moreover, distinguished from other members in class II of the HDAC family, HDAC6 contains 2 catalytic domains with the deacetylase activity and a specific ubiquitin-binding motif, the BUZ finger, at its C-terminus and plays roles in both deacetylse-related and ubiquitin-related regulations [41].”
BackgroundDevelopment of the first small molecule histone deacetylase 6 (HDAC6) degraders
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“Besides regulating cell motility, HDAC6 is also involved in the response of cells to various types of stress stimuli (Boyault et al, 2007b; Kawaguchi et al, 2003; Kwon et al, 2007), immune synapse organization, and the antigen- specific reorientation of the microtubule organizing center (MTOC)…”
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“Furthermore, HDAC6 is the only cytosolic HDAC with 2 catalytic domains.(34) The second domain is responsible mainly for its TDAC activity.”
BackgroundDevelopment of vorinostat: Current applications and future perspectives for cancer therapy
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“HDAC6 in particular appears to play a major role in the cytoplasm as it has been shown to deacetylate HSP90, a-tubulin, and cortactin as well as disrupt aggresome formation in the proteasome through its direct interaction with ubiquitin [15–21].”
BackgroundComprehensive lysine acetylomes emerging from bacteria to humans
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“deacetylase histone N-terminal tails, and repress gene expression (reviewed in [25]).”
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“HDAC6 warrants special attention as a HDAC predominantly, [11, 12] but not exclusively [9] localized to the”
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“…extend these data, we took advantage of 3T3 cell lines, previously established from mouse embryo fibroblasts isolated from parental (WT) or HDAC6-deficient (KO) mice, in which wild-type HDAC6 was re-expressed (þWT; Boyault et al, 2007b) and analysed the expression of murine SRSF2 by immunoblotting.”
BackgroundInfluentialSelf-citationThe Tale of Protein Lysine Acetylation in the Cytoplasm
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“The important role of HDAC6 in all of these different cellular defence mechanisms has been well described (for review see [76, 77]) and will not be discussed in detail in this paper.”
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“…deacetylation of other substrates as diverse as cortactin, Hsp90 or b -catenin, and also interacts with a broad spectrum of signalling partners, which underlies its role not only in migration but also in other cellular processes as well (Boyault et al , 2007; Valenzuela-Fernandez et al , 2008).”
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“HDAC6 belongs to the HDAC IIb family, which is closely related to a variety of diseases.(190) In 2018, Yang et al.”
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“In 1-d-old -syn fly brains, the immunostaining of -synuclein showed diffuse pattern (data not shown), which is similar to the case of young fly brains reported previously (Feany and Bender, 2000).”
BackgroundMethodInfluentialThe synergic effect of vincristine and vorinostat in leukemia in vitro and in vivo
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Structural Origin of Selectivity in Class II-Selective Histone Deacetylase Inhibitors
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“While HDAC6 plays multiple roles in the cytoplasm, very little is known about another cytoplasmic deacetylase, HDAC10, which is closest to HDAC6 (reviewed in [55]).”
BackgroundWilliams, K. A., Zhang, M., Xiang, S., Chen, H., Wu, J.-Y., Zhang, S., Ryan, M. B., Cox, A. D., Der, C. J., Fang, B., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.472506 · Cited by 112
Rao, R., Balusu, R., Fiskus, W. C., Mudunuru, U., Venkannagari, S., Chauhan, L., Smith, J. E., Hembruff, S. L., Ha, K., Atadja, P. W., et al. (2012) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-11-0979 · Cited by 112
HDAC11 is a regulator of diverse immune functions
Yanginlar, C., & Logie, C. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.12.002 · Cited by 112
Kerr, E. M., Holohan, C., McLaughlin, K. M., Majkut, J., Dolan, S., Redmond, K. M., Riley, J. S., McLaughlin, K. M., Stasik, I., Crudden, M. T. C. M., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.8 · Cited by 106
“HDAC6 is a unique HDAC that has key roles in regulating protein turnover by the proteasome through its regulation of HSP90 and by the aggresome through its ability to recruit polyubiquitinated proteins to the tubulin cytoskeleton.(26) Thus, this study identifies a further potential role for HDAC6 in regulating protein…”
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HDAC6 Deacetylates Ku70 and Regulates Ku70-Bax Binding in Neuroblastoma
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Richter‐Landsberg, C., & Leyk, J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1158-x · Cited by 106
“First α-tubulin was identified as a physiological substrate for HDAC6, and it was demonstrated that HDAC6 interacts with MTs and deacetylates them in vivo, thereby regulating MT dynamics ([93, 148], for review see [11]).”
BackgroundPKC alpha regulates Sendai virus‐mediated interferon induction through HDAC6 and β‐catenin
Zhu, J., Coyne, C. B., & Sarkar, S. N. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.351 · Cited by 103
“HDAC6 is a member of the class II histone deacetylase family enzymes that is present in the cytoplasm, and involved in multiple cellular processes (Cohen and Yao, 2004; Yang and Gregoire, 2005; Boyault et al, 2007).”
BackgroundHistone Deacetylase Inhibitors as Novel Anticancer Therapeutics
Walkinshaw, D. R., & Yang, X. (2008) · Current Oncology · doi:10.3747/co.v15i5.371 · Cited by 104
HDAC6 is required for invadopodia activity and invasion by breast tumor cells
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The Therapeutic Strategy of HDAC6 Inhibitors in Lymphoproliferative Disease
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KLF4 regulates adult lung tumor-initiating cells and represses K-Ras-mediated lung cancer
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“HDAC6 belongs to group IIb alongwith HDAC10, and it has unique structural and functional features.(51,52) We also treated cells with an HDAC6 inhibitor, ACY-1215,(53) but found no change in KLF4 expression (not shown).”
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“While most of the HDACs are localized in the nucleus, HDAC6 is a cytoplasmic protein associated with the cytoskeleton and involved in cytoskeleton-related activities (Boyault et al., 2007; Valenzuela-Fernández et al., 2008).”
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Heat Shock Protein 90 Inhibition in Lung Cancer
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Recent Advances in PROTACs for Drug Targeted Protein Research
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“Known substrates of HDAC6, including heat shock protein 90 and tubulin ( 24 ), showed increased acetylation by MS in the presence of BAS-2, validating our approach (Fig.”
Emerging approaches for histone deacetylase inhibitor drug discovery
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“This unique feature expounds its protective role against the accumulation of cytotoxic misfolded protein aggregates within cells [35].”
BackgroundInfluentialHDAC 6 at the Intersection of Neuroprotection and Neurodegeneration
d’Ydewalle, C. V. O., Bogaert, E., & Bosch, L. V. D. (2012) · Traffic · doi:10.1111/j.1600-0854.2012.01347.x · Cited by 75
“It has been suggested that an excess of HDAC6 favors the accumulation of ubiquitinated aggregates (67).”
BackgroundHistone Deacetylase 6 (HDAC6) Deacetylates Survivin for Its Nuclear Export in Breast Cancer
Riolo, M., Cooper, Z. A., Holloway, M. P., Cheng, Y., Bianchi, C. F., Yakirevich, E., Ma, L., Chin, Y. E., & Altura, R. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308791 · Cited by 75
Histone Deacetylase Inhibitors: The Epigenetic Therapeutics That Repress Hypoxia‐Inducible Factors
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“In addition, HDAC6 provides a link between protein acetylation and ubiquitination [164], suggesting a role in regulating protein stability.”
Metadata
- Authors
- Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S.
- Affiliations
- Inserm (FR)
- Corresponding author
- Khochbin, S
- Venue
- Oncogene
- Published
- 2007-08-13
- Volume
- 26
- Issue
- 37
- Pages
- 5468-5476
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2030185116
- Cited by
- 397
- References
- 85
- Citations by year
- 2026: 12 · 2025: 17 · 2024: 19 · 2023: 15 · 2022: 24 · 2021: 26 · 2020: 32 · 2019: 18 · 2018: 31 · 2017: 16 · 2016: 9 · 2015: 23 · 2014: 21 · 2013: 24 · 2012: 26
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Institut National Du Cancer
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- HDAC6, histone deacetylase, microtubule cytoskeleton, cytoskeleton, protein acetylation, ubiquitination, ubiquitin-binding domain, Hsp90 chaperone, signal transduction, stress response
- MeSH terms
- Acetylation, Animals, Cell Nucleus, Cytoskeleton, Enzyme Inhibitors, Histone Deacetylases, Humans, Protein Processing, Post-Translational, Signal Transduction, Protein Structure, Tertiary, Ubiquitin, Histone Deacetylase Inhibitors
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