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.
“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
HDAC6 is an attractive target for drug development and research.
“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]
HDAC6 seems to be very sensitive to PROTAC-mediated degradation, probably because of its dominant cytoplasmic localization.
“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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- 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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