Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
Open accessAbstract
Neurodegenerative tauopathies characterized by hyperphosphorylated tau include frontotemporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17) and Alzheimer's disease (AD). Reducing tau levels improves cognitive function in mouse models of AD and FTDP-17, but the mechanisms regulating the turnover of pathogenic tau are unknown. We found that tau is acetylated and that tau acetylation prevents degradation of phosphorylated tau (p-tau). We generated two antibodies specific for acetylated tau and showed that tau acetylation is elevated in patients at early and moderate Braak stages of tauopathy. Histone acetyltransferase p300 was involved in tau acetylation and the class III protein deacetylase SIRT1 in deacetylation. Deleting SIRT1 enhanced levels of acetylated-tau and pathogenic forms of p-tau, probably by blocking proteasome-mediated degradation. Inhibiting p300 with a small molecule promoted tau deacetylation and eliminated p-tau associated with tauopathy. Modulating tau acetylation could be a new therapeutic strategy to reduce tau-mediated neurodegeneration.
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Acetylation of tau is an early pathological feature of neurodegeneration; acetylated tau inhibits its degradation, promotes pathological aggregation and propagation, and contributes to tauopathy.
“In addition, the acetylation of tau is an early pathological feature of neurodegeneration. Acetylated tau inhibits its degradation, promotes pathological aggregation and propagation, and contributes to tauopathy [46–51].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [46]
The expression and activity of p300 are increased in the brain of AD patients, and dysregulation of p300/CBP promotes tau acetylation, which could aggravate tau accumulation and pathology.
“The expression and activity of p300 are increased in the brain of AD patients [179], and the dysregulation of p300/CBP promotes tau acetylation, which could aggravate tau accumulation and pathology [46, 48].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [46]
Tau acetylation reduces degradation of phosphorylated tau and increases tau pathology.
“Tau acetylation has been shown to reduce degradation of phosphorylated tau and increase tau pathology”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Min et al., 2010
Acetylation of tau inhibits its function and promotes pathological aggregation.
“Acetylation of tau inhibits its function and promotes pathological aggregation.373–375”
From Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell (2016) · cites this paper as [374]
Mass-spectrometry has proven valuable for locating PTMs implicated in CNS development and disorder, including p300-mediated acetylation of Tau and phosphorylation regulation of LSD1.
“For example, mass spectrometry has proven to be a valuable tool for locating PTMs implicated in CNS development37 and disorder38, including interrogating specific hypotheses such as the p300-mediated acetylation of Tau39 and the regulation of the transcriptional repressor LSD1 through phosphorylation40.”
From Decoding neuroproteomics: integrating the genome, translatome and functional anatomy (2014) · cites this paper as [39]
Acetylation contributes to tau pathology by inducing tau cleavage, preventing ubiquitin binding and impeding tau turnover.
“Acetylation also contributes to tau pathology by inducing tau cleavage, preventing ubiquitin binding and impeding tau turnover8,35.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [8]
Tau from patients with AD and other tauopathies is more heavily acetylated than in the brains of cognitively normal individuals.
“In addition to being hyperphosphorylated, tau from patients with AD and other tauopathies is more heavily acetylated than in the brains of cognitively normal individuals8.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [8]
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- Authors
- Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., Meyers, D., Cole, P. A., Ott, M., & Gan, L.
- Affiliations
- Gladstone Institutes (US)
- Icahn School of Medicine at Mount Sinai (US)
- University of California, San Francisco (US)
- Banner Sun Health Research Institute (US)
- University of California San Diego (US)
- Johns Hopkins University (US)
- Corresponding author
- Gan, Li
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 67
- Issue
- 6
- Pages
- 953-966
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3035103
- OpenAlex
- W1983523416
- Cited by
- 949
- References
- 52
- Citations by year
- 2026: 46 · 2025: 62 · 2024: 53 · 2023: 58 · 2022: 66 · 2021: 86 · 2020: 74 · 2019: 63 · 2018: 69 · 2017: 54 · 2016: 61 · 2015: 61 · 2014: 56 · 2013: 63 · 2012: 43
- FWCI
- 30.11
- Type
- journal article
- Language
- en
- Update notices
- erratum (2010-11-18)
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1050 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1c06rr018928-01)
- National Institute on Aging (R01AG030207, AG023501-06, P50AG023501)
- National Center for Research Resources (C06-RR-018928)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau acetylation, tauopathy, hyperphosphorylated tau, P300, SIRT1, proteasomal degradation, FTDP-17, Alzheimer's disease, frontotemporal dementia, Braak stages, histone acetyltransferase, protein deacetylation, tau-targeted therapy, neurodegeneration
- MeSH terms
- p300-CBP-Associated Factor, Acetylation, Analysis of Variance, Animals, Animals, Newborn, Carbazoles, Cells, Cultured, Cerebral Cortex, Cycloheximide, Disease Models, Animal, Enzyme Inhibitors, Gene Expression Regulation, Humans, Mice, Transgenic, Models, Biological, Mutation, Neurons, Phosphorylation, Protein Synthesis Inhibitors, Time Factors, Transfection, tau Proteins, Rats, Sprague-Dawley, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tauopathies, Immunoprecipitation, p300-CBP Transcription Factors, Mice, Rats, Ubiquitination, Sirtuin 1
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