Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss
Open accessAbstract
Tau toxicity has been implicated in the emergence of synaptic dysfunction in Alzheimer's disease (AD), but the mechanism by which tau alters synapse physiology and leads to cognitive decline is unclear. Here we report abnormal acetylation of K274 and K281 on tau, identified in AD brains, promotes memory loss and disrupts synaptic plasticity by reducing postsynaptic KIdney/BRAin (KIBRA) protein, a memory-associated protein. Transgenic mice expressing human tau with lysine-to-glutamine mutations to mimic K274 and K281 acetylation (tauKQ) exhibit AD-related memory deficits and impaired hippocampal long-term potentiation (LTP). TauKQ reduces synaptic KIBRA levels and disrupts activity-induced postsynaptic actin remodeling and AMPA receptor insertion. The LTP deficit was rescued by promoting actin polymerization or by KIBRA expression. In AD patients with dementia, we found enhanced tau acetylation is linked to loss of KIBRA. These findings suggest a novel mechanism by which pathogenic tau causes synaptic dysfunction and cognitive decline in AD pathogenesis.
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Acetylation of Tau at K281, a residue located in an F-actin interacting helix of Tau, affects the interaction of Tau with actin and modulates Tau-mediated toxicity.
“In addition to phosphorylation, acetylation of Tau at K281, a residues that is located in an F-actin interacting helix of Tau (Fig. 3d), affects the interaction of Tau with actin and modulate Tau-mediated toxicity26.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [26]
The Results report that an acetylation-mimicking K274/K281 tau mutant interacted less with F-actin than wild-type tau; the Discussion links that mutant to synaptic dysfunction and memory deficits. The paper does not establish that K281 alone has these effects or describe K281 as located in an F-actin-interacting helix. Its evidence for altered tau–actin binding comes from the double mutant, not directly from acetylated tau. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAcetylation of Tau modulates actin polymerization and enhances synaptic dysfunction.
“In addition, acetylation of Tau modulates actin polymerization and enhances synaptic dysfunction26.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [26]
Transgenic mice capable of acetylating K274 and K281 exhibited memory deficits and impairment of hippocampal long-term potentiation.
“The transgenic mice capable of acetylating K274 and K281 exhibited memory deficits and impairment of hippocampal long-term potentiation (LTP).”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [76]
Pathogenic tau acetylation causes synaptic dysfunction and cognitive decline in AD.
“This study led to a novel mechanism of pathogenic tau caused a role in causing synaptic dysfunction and cognitive decline in AD.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [76]
An increase in tau acetylation was linked to loss of KIBRA in AD patients with dementia.
“An increase in tau acetylation was linked to the loss of KIBRA in AD patients with dementia.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [76]
The LTP deficit could be saved by increasing actin polymerization or by expression of KIBRA protein.
“The LTP deficit could be saved by increasing the polymerization of actin or by expression of the KIBRA protein.”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [76]
Abnormal acetylation of K274 and K281 on tau in AD brains increases memory loss and disrupts synaptic plasticity by reducing postsynaptic KIBRA protein.
“Tracy et al. (2016) identified an abnormal acetylation of K274 and K281 on tau in AD brains, which increased memory loss and disrupted synaptic plasticity by reducing the postsynaptic KIBRA protein [76].”
From Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease (2020) · cites this paper as [76]
Lys280 acetylation enhances fibrillization, whereas Lys274 and Lys281 acetylation promotes tau distribution to the soma and dendrites, resulting in synaptic and cognitive dysfunction.
“Lys280 acetylation enhances fibrillization, whereas Lys274 and Lys281 acetylation promotes tau distribution to the soma and dendrites, and resulting in synaptic and cognitive dysfunction [157, 158, 160].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [157]
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 [157]
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 [157]
Acetylation of tau at Lys274, Lys280, and Lys281 residues within the microtubule binding domain impairs tau binding to microtubules.
“Specifically, acetylation of tau at Lys274, Lys280 and Lys281 residues within the microtubule binding domain impairs tau binding to microtubules.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [157]
Acetylation at Lys274, Lys280, Lys281, and Lys369 impairs tau function and is increased in Alzheimer's disease brains.
“In addition, acetylation at the Lys274, Lys280, Lys281, and Lys369 sites was shown to impair tau function and to be increased in AD brains [39].”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [39]
High levels of tau protein with acetylation at Lys163, Lys174, and Lys180, which inhibits degradation of hyperphosphorylated tau and contributes to accumulation of phosphorylated tau, are detected in brains of patients with mild to moderate Alzheimer's disease.
“High levels of tau protein with acetylation at the Lys163, Lys174, and Lys180 sites, which inhibits the degradation of hyperphosphorylated tau protein and thus contributes to the accumulation of phosphorylated tau protein, are detected in the brains of patients with mild to moderate AD.”
From Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review (2024) · cites this paper as [39]
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Jiang, N., Li, W., Jiang, S., Xie, M., & Liu, R. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115519 · Cited by 38 · see citing works
- Authors
- Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., Cong, X., Schilling, B., Ellerby, L. M., Huganir, R. L., & Gan, L.
- Affiliations
- Gladstone Institutes (US)
- Buck Institute for Research on Aging (US)
- Johns Hopkins University (US)
- Corresponding author
- Gan, Li
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2016-04
- Volume
- 90
- Issue
- 2
- Pages
- 245-260
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4859346
- OpenAlex
- W2327032644
- Cited by
- 277
- References
- 65
- Citations by year
- 2026: 24 · 2025: 33 · 2024: 24 · 2023: 27 · 2022: 24 · 2021: 34 · 2020: 27 · 2019: 27 · 2018: 35 · 2017: 16 · 2016: 6
- FWCI
- 22.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (1c06rr018928-01)
- National Institute on Aging (F32AG043301, R01AG030207, R01AG036884, R01AG051390)
- National Institute of Neurological Disorders and Stroke (R01NS040251, P30NS065780, RL1NS062413, R01NS036715)
- National Center for Research Resources (C06-RR-018928)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau acetylation, KIBRA, Alzheimer's disease, synaptic plasticity, long-term potentiation, memory loss, tauopathy, hippocampus, synaptic dysfunction
- MeSH terms
- Acetylation, Actins, Alzheimer Disease, Animals, Brain, Carrier Proteins, Hippocampus, Humans, Memory Disorders, Mice, Transgenic, Neuronal Plasticity, Phosphoproteins, Signal Transduction, tau Proteins, Long-Term Potentiation, Receptors, AMPA, Intracellular Signaling Peptides and Proteins, Mice, Primary Cell Culture
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