Roles of tau protein in health and disease
Open accessAbstract
Tau is well established as a microtubule-associated protein in neurons. However, under pathological conditions, aberrant assembly of tau into insoluble aggregates is accompanied by synaptic dysfunction and neural cell death in a range of neurodegenerative disorders, collectively referred to as tauopathies. Recent advances in our understanding of the multiple functions and different locations of tau inside and outside neurons have revealed novel insights into its importance in a diverse range of molecular pathways including cell signalling, synaptic plasticity, and regulation of genomic stability. The present review describes the physiological and pathophysiological properties of tau and how these relate to its distribution and functions in neurons. We highlight the post-translational modifications of tau, which are pivotal in defining and modulating tau localisation and its roles in health and disease. We include discussion of other pathologically relevant changes in tau, including mutation and aggregation, and how these aspects impinge on the propensity of tau to propagate, and potentially drive neuronal loss, in diseased brain. Finally, we describe the cascade of pathological events that may be driven by tau dysfunction, including impaired axonal transport, alterations in synapse and mitochondrial function, activation of the unfolded protein response and defective protein degradation. It is important to fully understand the range of neuronal functions attributed to tau, since this will provide vital information on its involvement in the development and pathogenesis of disease. Such knowledge will enable determination of which critical molecular pathways should be targeted by potential therapeutic agents developed for the treatment of tauopathies.
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Pathological tau disrupts synaptic integrity and neuronal connectivity, driving neurodegeneration and cognitive decline.
“Pathological tau, characterized by hyperphosphorylation and aggregation into neurofibrillary tangles, disrupts synaptic integrity and neuronal connectivity, driving neurodegeneration and cognitive decline.”
From Protective mechanisms against Alzheimer's disease in APOE3‐Christchurch homozygous astrocytes (2025) · cites this paper as [15]
In “Tau-mediated neurodegeneration > Axonal transport impairment in the tauopathies” (page unavailable), the review says pathological tau can compromise synapses and contribute to synaptic degeneration and neuronal demise. But “Tauopathies > Tau in neurofibrillary tangles and amyloid pathology” cautions that cognitive decline is not an inevitable result of tau pathology and that the mechanism linking synapse loss to cognitive decline is unidentified. The claim overstates a definite causal chain from pathological tau through disrupted connectivity to cognitive decline. (LLM, conf=0.86)
Experimental — accuracy not yet measuredVarious kinases are known to induce tau hyperphosphorylation, such as GSK-3β, a major tau kinase. These kinases are hyperactivated during the progression of AD and other tauopathies.
“Various kinases are known to induce tau hyperphosphorylation, such as GSK-3β, a major tau kinase. These kinases are hyperactivated during the progression of AD and other tauopathies [19], indicating that the development of their mediators may be an effective treatment for these diseases.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [19]
Truncation inhibits the ability of tau to bind to microtubules and promotes tau aggregation, mitochondrial dysfunction and synaptic deficits.
“Like phosphorylation and acetylation, truncation inhibits the ability of tau to bind to microtubules, and also promotes tau aggregation36,37, mitochondrial dysfunction37 and synaptic deficits39.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [37]
During characterization of PHFs isolated from the brains of individuals with AD, tau had undergone carboxy-terminal truncation by caspase-3.
“During the characterization of PHFs isolated from the brains of individuals with AD, it was discovered that tau had undergone carboxy-terminal truncation by caspase-336,37.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [37]
In cell and animal models, siRNA reduces tau pathology and associated functional impairments.
“In cell and animal models, siRNA was found to reduce tau pathology and associated functional impairments37.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [37]
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“The mechanistic role of PTMs in initiating Tau seeding and propagation still remains to be elucidated (Guo et al., 2017; Wang and Mandelkow, 2016).”
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- Authors
- Guo, T., Noble, W., & Hanger, D. P.
- Affiliations
- King's College London (GB)
- Corresponding author
- Hanger, Diane P.
- Venue
- Acta Neuropathologica
- Published
- 2017-04-06
- Volume
- 133
- Issue
- 5
- Pages
- 665-704
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC5390006
- OpenAlex
- W2605036205
- Cited by
- 1,003
- References
- 550
- Citations by year
- 2026: 87 · 2025: 120 · 2024: 112 · 2023: 112 · 2022: 118 · 2021: 154 · 2020: 115 · 2019: 88 · 2018: 75 · 2017: 21 · 2013: 1
- FWCI
- 10.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Acta Neuropathologica (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion, cc-by)
- Funders
- Alzheimer’s Research UK
- Alzheimer's Society
- Biotechnology and Biological Sciences Research Council
- National Centre for the Replacement, Refinement and Reduction of Animals in Research
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tau protein, tauopathy, tau aggregation, post-translational modification, tau mutations, tau propagation, axonal transport, synaptic dysfunction, mitochondrial dysfunction, unfolded protein response, protein degradation, synaptic plasticity, genome stability, neurodegeneration, neuronal loss
- MeSH terms
- Animals, Brain, Humans, Neurons, Protein Processing, Post-Translational, tau Proteins, Neurodegenerative Diseases, Tauopathies
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.
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