Interaction between Aβ and Tau in the Pathogenesis of Alzheimer’s Disease
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Extracellular neuritic plaques composed of amyloid‑β (Aβ) protein and intracellular neurofibrillary tangles containing phosphorylated tau protein are the two hallmark proteins of Alzheimer's disease (AD), and the separate neurotoxicity of these proteins in AD has been extensively studied. However, interventions that target Aβ or tau individually have not yielded substantial breakthroughs. The interest in the interactions between Aβ and tau in AD is increasing, but related drug investigations are in their infancy. This review discusses how Aβ accelerates tau phosphorylation and the possible mechanisms and pathways by which tau mediates Aβ toxicity. This review also describes the possible synergistic effects between Aβ and tau on microglial cells and astrocytes. Studies suggest that the coexistence of Aβ plaques and phosphorylated tau is related to the mechanism by which Aβ facilitates the propagation of tau aggregation in neuritic plaques. The interactions between Aβ and tau mediate cognitive dysfunction in patients with AD. In summary, this review summarizes recent data on the interplay between Aβ and tau to promote a better understanding of the roles of these proteins in the pathological process of AD and provide new insights into interventions against AD.
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Aβ oligomers promote tau phosphorylation and mislocalization by activating kinases such as GSK-3, CDK5, and Fyn kinase, and by interfering with tau degradation.
“For instance, Aβ oligomers promote tau phosphorylation and mislocalization by activating kinases such as GSK-3, CDK5, and Fyn kinase, and by interfering with tau degradation [50].”
From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [50]
The sections “Aβ accelerates the phosphorylation of tau protein” and “Aβ plaques facilitate neuritic plaque tau aggregation and propagation” describe Aβ-related tau phosphorylation involving GSK-3β, CDK-5, and Fyn. “Aβ also interferes with tau oligomerization” describes tau detaching from microtubules and possible redistribution, but does not establish the claimed mechanism of mislocalization. No passage found says Aβ oligomers interfere with tau degradation; the paper discusses tau cleavage and aggregation instead. Page numbers were unavailable in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThrough the cellular prion protein/mGluR5 complex, Aβ oligomers can trigger Fyn kinase activation, further driving tau toxicity.
“Through the cellular prion protein/mGluR5 complex, Aβ oligomers can trigger Fyn kinase activation, further driving tau toxicity [50].”
From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [50]
In “Aβ plaques facilitate neuritic plaque tau aggregation and propagation” (page unavailable), the review says Aβ oligomers initiate PrPC–Fyn-related tau phosphorylation and that Aβ and PrPC combine with an interaction partner to activate Fyn. It does not identify that partner as mGluR5, so the specified PrPC/mGluR5 complex is not supported by our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe main focus of AD therapies has been on removing or reducing Aβ plaques and tau tangles because they are characteristic of AD and thought important in onset and development.
“Since amyloid-beta (Aβ) plaques and tau tangles are characteristic of AD and are thought to be important in the onset and development of the disease, the main focus of these therapies has been on removing or reducing them.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [84]
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Zhang, Q., Li, T., Xu, M., Islam, B., & Wang, J. (2024) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-024-01486-1 · Cited by 25 · see citing works
A multi-targeting immunotherapy ameliorates multiple facets of Alzheimer’s disease in 3xTg mice
Feng, X., Hou, Y., Liu, J., Yan, F., Dai, M., Chen, M., Wang, J., Li, J., Liu, Z., Sun, D., et al. (2024) · npj Vaccines · doi:10.1038/s41541-024-00942-9 · Cited by 24 · see citing works
- Authors
- Zhang, H., Wei, W., Zhao, M., Ma, L., Jiang, X., Pei, H., Cao, Y., & Li, H.
- Affiliations
- Xiyuan Hospital (CN)
- Beijing University of Chinese Medicine (CN)
- Corresponding author
- Cao, Yu
- Li, Hao
- Venue
- International Journal of Biological Sciences
- Publisher
- Ivyspring International Publisher
- Published
- 2021
- Volume
- 17
- Issue
- 9
- Pages
- 2181-2192
- ISSN
- 1449-2288 (ISSN-L)
- PMC
- PMC8241728
- OpenAlex
- W3166313369
- Cited by
- 689
- References
- 185
- Citations by year
- 2026: 182 · 2025: 268 · 2024: 141 · 2023: 73 · 2022: 22 · 2021: 3
- FWCI
- 37.38
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- International Journal of Biological Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (81873350, 7202174)
- National Science and Technology Major Project
- 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, amyloid-beta, tau protein, tau phosphorylation, neuritic plaques, neurofibrillary tangles, microglia, astrocytes, tau aggregation, cognitive impairment, neurotoxicity
- MeSH terms
- Alzheimer Disease, Animals, Disease Models, Animal, Humans, Phosphorylation, Amyloid beta-Peptides, tau Proteins
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