Cited by 414Histone Deacetylase Inhibitors ResearchUbiquitin and proteasome pathwaysMicrotubule and mitosis dynamics

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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

Boyault, C, Sadoul, K, Pabion, M, Khochbin, S·2007·Oncogene

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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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“Moreover, HDACs also catalyze the deacetylation of non-histone proteins, involving transcription, cytoskeleton, and protein folding (Boyault et al. 2007).”
Histone Deacetylase Inhibitors Promising Therapeutic Target for Liver Diseases
Sharma, A., Sharma, U., & Gupta, S. (2025) · The International Journal of Gastroenterology and Hepatology Diseases · doi:10.2174/0126662906313034241223071431
Design, Synthesis, and Biological Evaluation of Indazole-Based Histone Deacetylase 6 InhibitorsPreprint
Ali, K. H., Gupta, S., Oh, Y. J., Hossain, M. M., Kim, J. H., Park, S. Y., & Seo, Y. H. (2025) · SSRN Electronic Journal · doi:10.2139/ssrn.5178961
Additional file 3 of Molecular mechanism and therapeutic potential of HDAC9 in intervertebral disc degeneration
Lei, M., Lin, H., Shi, D., Hong, P., Song, H. K., Herman, B., Liao, Z., & Yang, C. (2024) · Figshare · doi:10.6084/m9.figshare.26653233
Additional file 2 of Molecular mechanism and therapeutic potential of HDAC9 in intervertebral disc degeneration
Lei, M., Lin, H., Shi, D., Hong, P., Song, H. K., Herman, B., Liao, Z., & Yang, C. (2024) · Figshare · doi:10.6084/m9.figshare.24804777
Additional file 2 of The extracellular HDAC6 ZnF UBP domain modulates the actin network and post-translational modifications of Tau
Balmik, A. A., Sonawane, S. K., & Chinnathambi, S. (2021) · Figshare · doi:10.6084/m9.figshare.14525927
Rôle d'HDAC6 et de VCP dans la réponse au stress thermique. Implications dans l'IBMPFD
Pernet, L. (2014) · theses.fr (ABES) · doi:10.70675/47616bc9zd164z44b3z889cze4a70ebf46b9
The role of histone deacetylase 3 (HDAC3) during megakaryopoiesis
Ishaq, R. (2020) · theses.fr (ABES) · doi:10.70675/08096a2ez3ccaz4219za256zfb0a9d758e0e
Comparative DCMS analysis reveals a novel breed-specific X-linked selection signature in Changthangi sheep
Nath, S., Illa, S. K., Yata, V. K., Shukla, R., & Kolliputi, N. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2026.1774902
Development of novel quinoline derivatives as selective HDAC6 inhibitors exhibiting multiple anticancer effects
Peng, J., Zhao, Q., Yu, C., Liu, W., Yu, X., Qin, P., Liu, Y., Niu, H., Sun, J., Xue, H., et al. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110034
PI3K/HDAC Dual Inhibitors as Potential Anticancer Therapeutics: An Insight Into Design Strategies and Structure Activity Relationships
Dash, S., Shehensha, S., & Dhar, A. K. (2026) · ChemistrySelect · doi:10.1002/slct.73651 · Cited by 1
Zinc-finger ubiquitin-binding domain of histone deacetylase 6 modulates Tau structure and function
Balmik, A. A., & Chinnathambi, S. (2026) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2026.05.036
The extracellular Zinc-finger ubiquitin-binding domain of histone Deacetylase 6 enhances podosome formation in neuronal cells
Qureshi, T., Balmik, A. A., & Chinnathambi, S. (2026) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2026.05.060
HDAC6 is a biomarker of leukaemic dissemination and relapse in B-ALL
Jiménez-Camacho, K. E., Vargas‐Robles, H., Adomako, J., Sánchez-Argáez, A. B., Maximiliano, C. L., Sandoval-Cabrera, A., Dorantes-Acosta, E. M., Mejía‐Aranguré, J. M., Castañeda-Contreras, S., Núñez-Enríquez, J. C., et al. (2026) · British Journal of Cancer · doi:10.1038/s41416-026-03539-2
Integrated Multi-Omics Analysis and Experimental Validation Identify Acetylation-Related Genes as Potential Regulators in Osteoarthritis
Huang, Q., Zhao, X., Long, D., Li, M., Yiyi, J., Diao, H., Chen, W., & Meng, F. (2026) · Biomedicines · doi:10.3390/biomedicines14081806
“Histone acetyltransferases and histone deacetylases (HDACs) work together to fine-tune protein stability and transcriptional activity by regulating the acetylation status of non-histone proteins (e.g., transcription factors) [10,12,13].”
BindingDB Entry 50022509: Rational design and simple chemistry yield a superior, neuroprotective HDAC6 inhibitor, tubastatin A.
BindingDB (2025) · UC San Diego · doi:10.7270/q2nc65xr
BindingDB Entry 50023657: Synthesis and functional screening of novel inhibitors targeting the HDAC6 zinc finger ubiquitin-binding domain.
BindingDB (2026) · UC San Diego · doi:10.7270/q2c82g7g
BindingDB Entry 50017631: Discovery of HDAC6-Selective Inhibitor NN-390 with
BindingDB (2023) · UC San Diego · doi:10.7270/q2qv3rkm
BindingDB Entry 50020470: Selective and Bioavailable HDAC6 2-(Difluoromethyl)-1,3,4-oxadiazole Substrate Inhibitors and Modeling of Their Bioactivation Mechanism.
BindingDB (2024) · UC San Diego · doi:10.7270/q21z48vm
BindingDB Entry 2599: Structural Origin of Selectivity in Class II-Selective Histone Deacetylase Inhibitors
BindingDB (2008) · UC San Diego · doi:10.7270/q2nc5zg2

Authors: Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S.
Affiliations: Inserm (FR)
Corresponding author: Khochbin, S
ORCID: Boyault, C
Sadoul, K
Khochbin, S
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2007-08-13
Volume: 26
Issue: 37
Pages: 5468-5476
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1210614
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

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