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Tau protein kinases: Involvement in Alzheimer's disease
Abstract
Tau phosphorylation is regulated by a balance between tau kinase and phosphatase activities. Disruption of this equilibrium was suggested to be at the origin of abnormal tau phosphorylation and thereby might contribute to tau aggregation. Thus, understanding the regulation modes of tau phosphorylation is of high interest in determining the possible causes at the origin of the formation of tau aggregates in order to elaborate protection strategies to cope with these lesions in Alzheimer's disease. Among the possible and specific interventions that reverse tau phosphorylation is the inhibition of certain tau kinases. Here, we extensively reviewed tau protein kinases, their physiological roles and regulation, their involvement in tau phosphorylation and their relevance to AD. We also reviewed the most common inhibitory compounds acting on each tau kinase.
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“The GSK3β can orchestrate pathological tau-phosphorylation at over two-dozen disease-associated sites [181–184].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [184]
In the citing paper
“Different kinases have been demonstrated to be involved in Tau phosphorylation, including the glycogen synthase kinase 3β (GSK-3β), protein kinase A, p38 mitogen activated protein kinase (MAPK), extracellular signal-related kinases (Erk1/2), and c-Jun N-terminal kinases (JNK) 1/3 (Martin et al., 2013).”
From Exploring the Therapeutic Potential of Phytochemicals in Alzheimer’s Disease: Focus on Polyphenols and Monoterpenes (2022) · cites this paper as Martin et al., 2013
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Kurkute, P., Sonawane, S., Pratyush, K., Dravyakar, B. R., Ansari, A., Bawane, P. P., Agrawal, Y. O., Khairnar, M. V., & Siddique, M. U. M. (2025) · Current Computer - Aided Drug Design · doi:10.2174/0115734099366145250526081959
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Zhong, Q., Chen, Y., & Jiang, R. (2025) · Journal of Visualized Experiments · doi:10.3791/68884
Metadata
- Authors
- Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F.
- Affiliations
- Inserm (FR)
- Centre Hospitalier Universitaire de Limoges (FR)
- Université de Limoges (FR)
- Corresponding author
- Martin, Ludovic
- ORCID
- Venue
- Ageing Research Reviews
- Publisher
- Elsevier BV
- Published
- 2013-01
- Volume
- 12
- Issue
- 1
- Pages
- 289-309
- ISSN
- 1568-1637 (ISSN-L)
- OpenAlex
- W1988332799
- Cited by
- 631
- References
- 326
- Citations by year
- 2026: 24 · 2025: 62 · 2024: 64 · 2023: 51 · 2022: 79 · 2021: 53 · 2020: 56 · 2019: 46 · 2018: 55 · 2017: 24 · 2016: 34 · 2015: 26 · 2014: 37 · 2013: 17
- FWCI
- 2.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Ageing Research Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Université de Nantes
- Conseil Régional du Limousin
- Institut National de la Santé et de la Recherche Médicale
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Aldose Reductase and Taurine
- Keywords
- tau phosphorylation, Alzheimer's disease, tau aggregation, kinase inhibition, kinase inhibitors
- MeSH terms
- Alzheimer Disease, Animals, Humans, Phosphorylation, Protein-Tyrosine Kinases, tau Proteins, Glycogen Synthase Kinase 3, Proline-Directed Protein Kinases
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