Histone deacetylase 6 inhibition compensates for the transport deficit in Huntington's disease by increasing tubulin acetylation
Open accessAbstract
A defect in microtubule (MT)-based transport contributes to the neuronal toxicity observed in Huntington's disease (HD). Histone deacetylase (HDAC) inhibitors show neuroprotective effects in this devastating neurodegenerative disorder. We report here that HDAC inhibitors, including trichostatin A (TSA), increase vesicular transport of brain-derived neurotrophic factor (BDNF) by inhibiting HDAC6, thereby increasing acetylation at lysine 40 of alpha-tubulin. MT acetylation in vitro and in cells causes the recruitment of the molecular motors dynein and kinesin-1 to MTs. In neurons, acetylation at lysine 40 of alpha-tubulin increases the flux of vesicles and the subsequent release of BDNF. We show that tubulin acetylation is reduced in HD brains and that TSA compensates for the transport- and release-defect phenotypes that are observed in disease. Our findings reveal that HDAC6 inhibition and acetylation at lysine 40 of alpha-tubulin may be therapeutic targets of interest in disorders such as HD in which intracellular transport is altered.
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HDAC6 primarily targets cytoplasmic substrates such as microtubules, thereby influencing cytoskeletal dynamics and axonal transport.
“Certain isoforms exhibit specialized functions; for instance, HDAC6 primarily targets cytoplasmic substrates such as microtubules, thereby influencing cytoskeletal dynamics and axonal transport (Dompierre et al., 2007).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Dompierre et al., 2007
The section on HDAC6-dependent transport identifies HDAC6 as cytoplasmic and reports that it preferentially deacetylates tubulin over histone H3. The Discussion says HDAC6 inhibition increases microtubule acetylation and stimulates axonal transport. But Table 1 explicitly states that microtubule dynamics are not affected by acetylation, so the claim about influencing cytoskeletal dynamics is not supported in that sense. (LLM, conf=0.87)
Experimental — accuracy not yet measuredCytoplasmic dynein transports cargo toward the minus end of MT and binds preferably to acetylated MTs like kinesins.
“Since cytoplasmic dynein transports cargo toward the minus end of MT and binds preferably to acetylated MTs like kinesins (16, 17)”
From Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons (2026) · cites this paper as [17]
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- Authors
- Dompierre, J. P., Godin, J. D., Charrin, B. C., Cordelières, F. P., King, S. J., Humbert, S., & Saudou, F.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of Missouri–Kansas City (US)
- ORCID
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2007-03-28
- Volume
- 27
- Issue
- 13
- Pages
- 3571-3583
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6672116
- OpenAlex
- W2012887006
- Cited by
- 792
- References
- 64
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- FWCI
- 17.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Open Repository and Bibliography (University of Liège) (submittedVersion)
- Funders
- Association pour la Recherche sur le Cancer
- Agence Nationale de la Recherche (018-01)
- Institut National de la Santé et de la Recherche Médicale
- BNP Paribas Cardif
- National Institutes of Health
- Fondation BNP Paribas
- National Institute of Mental Health (MH.NS 31862)
- National Cancer Institute
- National Institute of Neurological Disorders and Stroke (R01NS048501, NS 48501)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- Huntington's disease, HDAC6, HDAC6 inhibition, trichostatin A, tubulin acetylation, microtubule transport, vesicle trafficking, brain-derived neurotrophic factor, BDNF release, dynein, kinesin-1, neurodegeneration, neuroprotection
- MeSH terms
- Histone Deacetylase 6, Vorinostat, Acetylation, Animals, Biological Transport, Active, Cell Line, Cells, Cultured, Cerebral Cortex, Histone Deacetylases, Huntington Disease, Hydroxamic Acids, Microtubules, Tubulin, Visual Cortex, Neuroprotective Agents, Microscopy, Video, Brain-Derived Neurotrophic Factor, Molecular Motor Proteins, Transport Vesicles, Mice, Histone Deacetylase Inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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