Site-specific phosphorylation of tau inhibits amyloid-β toxicity in Alzheimer’s mice
Abstract
Tau phosphorylation—not all bad: Alzheimer's disease presents with amyloid-β (Aβ) plaques and tau tangles. The prevailing idea in the field is that Aβ induces phosphorylation of tau, which in turn mediates neuronal dysfunction. Working in Alzheimer's disease mouse models, Ittner et al. found evidence for a protective role of tau in early Alzheimer's disease. This protection involves specific tau phosphorylation at threonine 205 at the postsynapse. A protective role of phosphorylated tau in disease challenges the dogma that tau phosphorylation only mediates toxic processes. Science , this issue p. 904
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Tau phosphorylation at T205 reduces the association of tau to PSD95/NMDAR complexes and therefore limits Aβ-induced excitotoxicity.
“Tau phosphorylation at T205 has been shown to reduce the association of tau to postsynaptic density-95 (PSD95)/NMDAR complexes and therefore to limit Aβ-induced excitotoxicity [144].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [144]
The rise in pT205/T205 associated with declining synaptic homeostasis could be a protective process that increases T205 phosphorylation under synaptic distress from chronic Aβ exposure, at least in DIAD.
“Our findings of an increase in pT205/T205 being associated with a decline in synaptic homeostasis could represent a protective process resulting in increased phosphorylation at T205 with synaptic distress from chronic Aß exposure, at least in DIAD51.”
From A soluble phosphorylated tau signature links tau, amyloid and the evolution of stages of dominantly inherited Alzheimer’s disease (2020) · cites this paper as [51]
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- Authors
- Ittner, A., Chua, S. W., Bertz, J., Volkerling, A., van der Hoven, J., Gladbach, A., Przybyla, M., Bi, M., van Hummel, A., Stevens, C. H., Ippati, S., Suh, L. S., Macmillan, A., Sutherland, G., Kril, J. J., Silva, A. P. G., Mackay, J. P., Poljak, A., Delerue, F., Ke, Y. D., & Ittner, L. M.
- Affiliations
- UNSW Sydney (AU)
- Dementia Research Unit, School of Medical Sciences, University of New South Wales (UNSW), Sydney, New South Wales 2052, Australia.
- The University of Sydney (AU)
- Corresponding author
- Ittner, Arne
- Ittner, Lars M.
- ORCID
- Venue
- Science
- Published
- 2016-11-18
- Volume
- 354
- Issue
- 6314
- Pages
- 904-908
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2554598802
- Cited by
- 263
- References
- 53
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 20 · 2023: 25 · 2022: 27 · 2021: 43 · 2020: 36 · 2019: 22 · 2018: 39 · 2017: 30
- FWCI
- 24.43
- Type
- journal article
- Language
- en
- Update notices
- correction (2025-12-11)
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Research Online (University of Wollongong) (submittedVersion)
- Funders
- National Health and Medical Research Council (1081916, 1037746, 1003083)
- Australian Research Council (DP130102027, DE130101591)
- Alzheimer's Association (NIRG000070035)
- Alzheimer's Australia (DGP14-39, DGP14-95)
- NIH (R28AA012725)
- UNSW Australia
- 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, amyloid-beta toxicity, Alzheimer's disease, p38 MAPK, p38γ, excitotoxicity, postsynaptic signaling, neuronal cell death, cognitive impairment, mouse models of Alzheimer's disease
- MeSH terms
- Disks Large Homolog 4 Protein, Alzheimer Disease, Animals, Cognition Disorders, Disease Models, Animal, Membrane Proteins, Mice, Transgenic, Neurons, Neurotoxins, Phosphorylation, Signal Transduction, Amyloid beta-Peptides, tau Proteins, Mitogen-Activated Protein Kinase 12, Mice, Guanylate Kinases
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