Tau in physiology and pathology
Abstract
Tau is a microtubule-associated protein that has a role in stabilizing neuronal microtubules and thus in promoting axonal outgrowth. Structurally, tau is a natively unfolded protein, is highly soluble and shows little tendency for aggregation. However, tau aggregation is characteristic of several neurodegenerative diseases known as tauopathies. The mechanisms underlying tau pathology and tau-mediated neurodegeneration are debated, but considerable progress has been made in the field of tau research in recent years, including the identification of new physiological roles for tau in the brain. Here, we review the expression, post-translational modifications and functions of tau in physiology and in pathophysiology.
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This list essentially covers all previously known Tau kinases (n = ~11).
“Remarkably, this list essentially covers all previously known Tau kinases (n = ~11) (Wang and Mandelkow, 2016).”
From Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer’s Disease Progression (2020) · cites this paper as Wang and Mandelkow, 2016
Under pathological conditions, hyperphosphorylation of tau reduces its affinity for tubulin and is thought to drive abnormal aggregations of phosphorylated tau, such as neuropil threads or neurofibrillary tangles, resulting in tauopathies.
“However, under pathological conditions, the hyperphosphorylation of tau reduces its affinity for tubulin and is thought to drive abnormal aggregations of phosphorylated tau (p-tau), such as neuropil threads or neurofibrillary tangles (NFTs), resulting in tauopathies (Wang and Mandelkow, 2016; Kovacs, 2017).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Wang and Mandelkow, 2016
Tau is a microtubule-associated protein that binds and promotes assembly of microtubules in neurons under physiological conditions.
“Tau is a microtubule-associated protein known to bind and promote assembly of microtubules in neurons under physiological conditions.”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Wang and Mandelkow, 2016
PP2A is estimated to account for 70% of human brain tau dephosphorylation.
“which is estimated to account for 70% of human brain tau dephosphorylation (Wang and Mandelkow, 2016).”
From Tauopathy and Epilepsy Comorbidities and Underlying Mechanisms (2022) · cites this paper as Wang and Mandelkow, 2016
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 [35]
N-glycosylation of tau is increased in AD and is thought to promote phosphorylation and pathological conformational changes.
“Conversely, N-glycosylation of tau, which is thought to promote phosphorylation and pathological conformational changes, is increased in AD9,35.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [35]
Tauopathies include neurological disorders such as Alzheimer disease, frontotemporal dementia and progressive supranuclear palsy, in which pathology is heavily associated with toxic accumulation of aberrant tau species, leading tau to aggregate into paired helical filaments and ultimately into neurofibrillary tangles that result in neuronal cell death.
“Tauopathies include neurological disorders, such as Alzheimer disease, frontotemporal dementia (FTD) and progressive supranuclear palsy (PSP)182, in which pathology is heavily associated with toxic accumulation of aberrant tau species, leading tau to aggregate into paired helical filaments and ultimately into neurofibrillary tangles that result in neuronal cell death183.”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [182]
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- Authors
- Wang, Y., & Mandelkow, E.
- Affiliations
- Center of Advanced European Studies and Research (DE)
- Corresponding author
- Wang, Yipeng
- ORCID
- Wang, Yipeng
- Venue
- Nature Reviews Neuroscience
- Published
- 2015-12-03
- Volume
- 17
- Issue
- 1
- Pages
- 22-35
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- OpenAlex
- W2185034389
- Cited by
- 2,251
- References
- 47
- Citations by year
- 2026: 255 · 2025: 276 · 2024: 253 · 2023: 240 · 2022: 228 · 2021: 244 · 2020: 231 · 2019: 174 · 2018: 173 · 2017: 115 · 2016: 60 · 2013: 1
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- DZNE Pub (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust
- 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, microtubule stabilization, tauopathy, tau aggregation, neurodegeneration, post-translational modification, intrinsically disordered proteins, axon growth
- MeSH terms
- Animals, Humans, Phosphorylation, Protein Processing, Post-Translational, tau Proteins, Tauopathies
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