Tau phosphorylation: the therapeutic challenge for neurodegenerative disease
Abstract
The microtubule-associated protein tau is integral to the pathogenesis of Alzheimer's disease (AD), as well as several related disorders, termed tauopathies, in which tau is deposited in affected brain regions. In the tauopathies, pathological tau is in an elevated state of phosphorylation and is aberrantly cleaved. It also exhibits abnormal conformations and becomes aggregated, resulting in neurofibrillary tau pathology. Recent evidence suggests that relatively early disease-associated changes in soluble tau proteins, including phosphorylation, are involved in the induction of neuronal death. Here, we summarize recent developments that suggest new therapeutic strategies to prevent or reduce the progression of pathology in the tauopathies. A list of tau phosphorylation sites identified in the tauopathies and in controls accompanies this review.
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More than 45 tau residues were found phosphorylated at higher frequencies in post-mortem brain tissue from Alzheimer's disease patients.
“Of which >45 residues were found to be phosphorylated at higher frequencies in post-mortem brain tissue from Alzheimer’s disease patients (Morishima-Kawashima et al., 1995; Hanger et al., 2007; Hanger et al., 2009; Wesseling et al., 2020).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Hanger et al., 2009
Tau contains ~85 predicted phosphorylation sites.
“Tau contains ~85 predicted phosphorylation sites (Hanger et al., 2009; Chakraborty et al., 2024).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Hanger et al., 2009
AT8 recognizes Tau phosphorylated at Ser202 and Thr205 or at Ser199, Ser202, and Thr205.
“AT8, which recognizes Tau that is phosphorylated at Ser202 and Thr205 (Goedert et al., 1995) or Ser199, Ser202, and Thr205 (Hanger et al., 2009).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Hanger et al., 2009
Tau is a phosphoprotein whose functions can be regulated by phosphorylation.
“Tau is also a phosphoprotein, the functions of which can be regulated by phosphorylation (Stoothoff and Johnson, 2005;Hanger et al., 2009).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Hanger et al., 2009
AT8 reactivity has been frequently used as an indicator of hyperphosphorylation of Tau in AD brains or other tauopathies.
“AT8 reactivity has been frequently used as an indicator of hyperphosphorylation of Tau in AD brains or other tauopathies (Stoothoff and Johnson, 2005;Hanger et al., 2009).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Hanger et al., 2009
Detection by AT8 is commonly used as a marker of abnormal phosphorylation in brains of Alzheimer's patients.
“their detection by this antibody is commonly used as a marker of abnormal phosphorylation in brains of Alzheimer's patients.”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Hanger et al., 2009
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- Authors
- Hanger, D. P., Anderton, B. H., & Noble, W.
- Affiliations
- King's College London (GB)
- Corresponding author
- Hanger, Diane P.
- Venue
- Trends in Molecular Medicine
- Publisher
- Elsevier BV
- Published
- 2009-03
- Volume
- 15
- Issue
- 3
- Pages
- 112-119
- ISSN
- 1471-4914 (ISSN-L)
- OpenAlex
- W2112136536
- Cited by
- 965
- References
- 10
- Citations by year
- 2026: 54 · 2025: 63 · 2024: 46 · 2023: 55 · 2022: 75 · 2021: 73 · 2020: 74 · 2019: 51 · 2018: 62 · 2017: 62 · 2016: 55 · 2015: 38 · 2014: 41 · 2013: 62 · 2012: 50
- FWCI
- 5.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Molecular Medicine (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- Research Councils UK
- Medical Research Council
- 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 phosphorylation, tauopathy, Alzheimer's disease, neurofibrillary tangles, tau aggregation, tau cleavage, tau conformation, neuronal cell death, tau phosphorylation sites, treatment options, neurodegenerative diseases
- MeSH terms
- Animals, Humans, Phosphorylation, Phosphotransferases, tau Proteins, Tauopathies
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