Histone deacetylase 6 interacts with the microtubule‐associated protein tau
Open accessAbstract
Histone deacetylase 6 (HDAC6), a unique cytoplasmic deacetylase, likely plays a role in neurodegeneration by coordinating cell responses to abnormal protein aggregation. Here, we provide in vitro and in vivo evidence that HDAC6 interacts with tau, a microtubule‐associated protein that forms neurofibrillary tangles in Alzheimer’s disease. This interaction is mediated by the microtubule‐binding domain on tau and the Ser/Glu tetradecapeptide domain on HDAC6. Treatment with tubacin, a selective inhibitor of tubulin deacetylation activity of HDAC6, did not disrupt HDAC6–tau interaction. Nonetheless tubacin treatment attenuated site‐specific tau phosphorylation, as did shRNA‐mediated knockdown of HDAC6. Proteasome inhibition potentiated HDAC6–tau interactions and facilitated the concentration and co‐localization of HDAC6 and tau in a perinuclear aggresome‐like compartment, independent of HDAC6 tubulin deacetylase activity. Furthermore, we observed that in Alzheimer’s disease brains the protein level of HDAC6 was significantly increased. These findings establish HDAC6 as a tau‐interacting protein and as a potential modulator of tau phosphorylation and accumulation.
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Increased Tau acetylation reduces Tau phosphorylation.
“while increased Tau acetylation reduces Tau phosphorylation [34, 42].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [34]
The Results report that HDAC6 inhibition reduced tau phosphorylation at T231 in cell-culture models, but not at all sites tested (page not provided). The Discussion describes acetylation of α-tubulin as a possible indirect mechanism; it does not show that increased acetylation of tau caused the reduction. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHDAC6 expression is increased in the cortex and hippocampus of AD patients.
“Expression of HDAC6 is increased in the cortex and hippocampus of AD patients [34–36].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [34]
Increased levels of HDAC2 and HDAC6 are detected in AD mouse models and AD patients.
“In addition, increased levels of HDAC2 and HDAC6 were detected in AD mouse models and AD patients.296,297”
From Microbiota–gut–brain axis and its therapeutic applications in neurodegenerative diseases (2024) · cites this paper as [297]
Histone deacetylase 6 interacts with the microtubule-associated protein tau.
“Histone deacetylase 6 interacts with the microtubule‐associated protein tau 25.”
From Altered Machinery of Protein Synthesis in Alzheimer's: From the Nucleolus to the Ribosome (2016) · cites this paper as [25]
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- Authors
- Ding, H., Dolan, P. J., & Johnson, G. V. W.
- Affiliations
- University of Alabama at Birmingham (US)
- University of Rochester Medicine (US)
- Corresponding author
- Johnson, Gail V. W.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2008-08-11
- Volume
- 106
- Issue
- 5
- Pages
- 2119-2130
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC2574575
- OpenAlex
- W2013037750
- Cited by
- 387
- References
- 49
- Citations by year
- 2026: 15 · 2025: 26 · 2024: 33 · 2023: 29 · 2022: 18 · 2021: 31 · 2020: 23 · 2019: 26 · 2018: 22 · 2017: 22 · 2016: 18 · 2015: 27 · 2014: 29 · 2013: 21 · 2012: 18
- FWCI
- 6.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Rochester
- National Institutes of Health
- Medical Center, University of Rochester
- National Institute on Aging (P50 AG 16582, P50AG016582)
- National Cancer Institute
- National Institute of Neurological Disorders and Stroke (NS051279, R01NS051279)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Health Sciences › Medicine › Pharmacology › Cholinesterase and Neurodegenerative Diseases
- Keywords
- HDAC6, tau protein, protein-protein interaction, microtubule-binding domain, tubacin, tubulin deacetylation, tau phosphorylation, aggresomes, proteasome inhibition, neurofibrillary tangles, Alzheimer's disease, neurodegeneration, protein aggregation
- MeSH terms
- Histone Deacetylase 6, Aged, Alzheimer Disease, Anilides, Brain, Cell Compartmentation, Cell Line, Enzyme Inhibitors, Female, Histone Deacetylases, Humans, Hydroxamic Acids, Male, Microtubules, Middle Aged, Neurons, Phosphorylation, Protein Binding, Organelles, Down-Regulation, Neurofibrillary Tangles, tau Proteins, Protein Structure, Tertiary, RNA, Small Interfering
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