Alzheimer’s disease: Ablating single master site abolishes tau hyperphosphorylation
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Hyperphosphorylation of the neuronal tau protein is a hallmark of neurodegenerative tauopathies such as Alzheimer’s disease. A central unanswered question is why tau becomes progressively hyperphosphorylated. Here, we show that tau phosphorylation is governed by interdependence— a mechanistic link between initial site-specific and subsequent multi-site phosphorylation. Systematic assessment of site interdependence identified distinct residues (threonine-50, threonine-69, and threonine-181) as master sites that determine propagation of phosphorylation at multiple epitopes. CRISPR point mutation and expression of human tau in Alzheimer’s mice showed that site interdependence governs physiologic and amyloid-associated multi-site phosphorylation and cognitive deficits, respectively. Combined targeting of master sites and p38α, the most central tau kinase linked to interdependence, synergistically ablated hyperphosphorylation. In summary, our work delineates how complex tau phosphorylation arises to inform therapeutic and biomarker design for tauopathies.
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Co-targeting p38α and the master sites synergistically eliminated hyperphosphorylation of tau.
“Co-targeting p38α, the most central tau kinase associated with interdependence, and the master sites synergistically eliminated hyperphosphorylation of tau [39].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [39]
Tau phosphorylation is controlled by interdependence, where initial site-specific phosphorylation at master sites leads to subsequent multi-site phosphorylation.
“A recent study demonstrated that tau phosphorylation is controlled by interdependence, an initial site-specific phosphorylation (they called “master sites”) leads to subsequent multi-site phosphorylation.”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [39]
p38α MAPK is a key kinase involved in microglia-induced neuroinflammation leading to tau pathology, and this kinase can also directly regulate tau phosphorylation.
“As mentioned above, p38α MAPK is a key kinase involved in microglia-induced neuroinflammation leading to tau pathology [135, 137], and this kinase can also directly regulate tau phosphorylation [39].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [39]
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- Authors
- Stefanoska, K., Gajwani, M., Tan, A. R. P., Ahel, H. I., Asih, P. R., Volkerling, A., Poljak, A., & Ittner, A.
- Affiliations
- Flinders University (AU)
- Monash University (AU)
- The University of Sydney (AU)
- UNSW Sydney (AU)
- Corresponding author
- Stefanoska, Kristie
- Ittner, Arne
- ORCID
- Venue
- Science Advances
- Published
- 2022-07-08
- Volume
- 8
- Issue
- 27
- Pages
- eabl8809-eabl8809
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC9258953
- OpenAlex
- W4286246004
- Cited by
- 128
- References
- 74
- Citations by year
- 2026: 30 · 2025: 38 · 2024: 33 · 2023: 25 · 2022: 2
- FWCI
- 15.31
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- 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
- Alzheimer's disease, tau hyperphosphorylation, tauopathy, cognitive impairment, biomarkers
- MeSH terms
- Alzheimer Disease, Animals, Humans, Phosphorylation, Threonine, tau Proteins, Tauopathies, Mice
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