Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
Open accessAbstract
Tauopathies, including frontotemporal dementia (FTD) and Alzheimer's disease (AD), are neurodegenerative diseases in which tau fibrils accumulate. Recent evidence supports soluble tau species as the major toxic species. How soluble tau accumulates and causes neurodegeneration remains unclear. Here we identify tau acetylation at Lys174 (K174) as an early change in AD brains and a critical determinant in tau homeostasis and toxicity in mice. The acetyl-mimicking mutant K174Q slows tau turnover and induces cognitive deficits in vivo. Acetyltransferase p300-induced tau acetylation is inhibited by salsalate and salicylate, which enhance tau turnover and reduce tau levels. In the PS19 transgenic mouse model of FTD, administration of salsalate after disease onset inhibited p300 activity, lowered levels of total tau and tau acetylated at K174, rescued tau-induced memory deficits and prevented hippocampal atrophy. The tau-lowering and protective effects of salsalate were diminished in neurons expressing K174Q tau. Targeting tau acetylation could be a new therapeutic strategy against human tauopathies.
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Tau acetylation at Lys280 can only be detected in AD and 4R tauopathies such as corticobasal degeneration and PSP.
“Acetylation of tau at Lys174, Lys274, Lys280, and Lys281 have been well characterized due to their association with AD: tau acetylation at Lys280 can only be detected in AD and 4R tauopathies such as corticobasal degeneration and PSP.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [156]
Increased levels of acetylated tau at Lys174, Lys274, and Lys281 have been observed in the brain of AD patients at varying disease stages.
“Additionally, increased levels of acetylated tau at Lys174, Lys 274, and Lys281 have been observed in the brain of AD patients at varying disease stages [156–159].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [156]
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 [48]
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 [48]
Tau is acetylated by the lysine acetyltransferase p300 and its close homolog CREB-binding protein (CBP).
“Tau is acetylated by the lysine acetyltransferase p300 and its close homolog CREB-binding protein (CBP) [48].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [48]
In preclinical testing, salsalate reduced p300 HAT activity, leading to reduced tau pathology, preserved hippocampal volume and improved cognition in transgenic mice.
“In preclinical testing, salsalate reduced p300 HAT activity, leading to reduced tau pathology, preserved hippocampal volume and improved cognition in transgenic mice.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [132]
Early tau post-translational modifications lead to misfolding, mislocalization, oligomerization, and changes in solubility, and these events appear to be determinant toxicity effectors.
“Cumulative evidence from murine tauopathy models and postmortem patient brain studies suggests that early tau post-translational modifications lead to misfolding, mislocalization, oligomerization, and changes in solubility. These events appear to be determinant toxicity effectors”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Min et al., 2015
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- Authors
- Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., Sohn, P. D., Schilling, B., Cong, X., Ellerby, L., Gibson, B. W., Johnson, J., Krogan, N., Shamloo, M., Gestwicki, J., Masliah, E., Verdin, E., & Gan, L.
- Affiliations
- Gladstone Institutes (US)
- Stanford Medicine (US)
- University of California, San Francisco (US)
- Buck Institute for Research on Aging (US)
- University of California San Diego (US)
- Corresponding author
- Verdin, Eric
- Gan, Li
- ORCID
- Venue
- Nature Medicine
- Published
- 2015-09-21
- Volume
- 21
- Issue
- 10
- Pages
- 1154-1162
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- PMC
- PMC4598295
- OpenAlex
- W2182763281
- Cited by
- 516
- References
- 61
- Citations by year
- 2026: 39 · 2025: 37 · 2024: 39 · 2023: 43 · 2022: 38 · 2021: 58 · 2020: 57 · 2019: 51 · 2018: 56 · 2017: 46 · 2016: 42 · 2015: 8 · 2014: 1
- FWCI
- 37.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Medicine (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute on Aging (R01AG030207, P50AG005131, R01AG036884)
- National Institute of Mental Health (P30MH062512)
- National Institute of Allergy and Infectious Diseases (P30AI027763)
- National Institute of Diabetes and Digestive and Kidney Diseases (R24DK085610)
- National Institute of Neurological Disorders and Stroke (R01NS040251, P30NS065780, NS40251, RL1NS062413, NS062413, R01NS059690)
- National Center for Research Resources (S10RR024615)
- 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, Alzheimer's disease, frontotemporal dementia, P300, salsalate, salicylates, memory impairment, hippocampal atrophy, tau-targeted therapy, transgenic mouse model
- MeSH terms
- Acetylation, Animals, Behavior, Animal, Cognition Disorders, Humans, tau Proteins, Neurodegenerative Diseases, Mice
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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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