Cited by 646Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchAldose Reductase and Taurine

Tau protein kinases: Involvement in Alzheimer's disease

Martin, Ludovic, Latypova, Xenia, Wilson, Cornelia M., Magnaudeix, Amandine, Perrin, Marie-Laure, Yardin, Catherine, Terro, Faraj·2013·Ageing Research Reviews

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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Crossref · 10.1016/j.arr.2012.06.003

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324 of 324 references verified0 citation errors · 0 not checkable

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  • GSK3β can orchestrate pathological tau phosphorylation at over two-dozen disease-associated sites.

    “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]

  • Different kinases are involved in Tau phosphorylation, including GSK-3β, protein kinase A, p38 MAPK, Erk1/2, and JNK1/3.

    “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).”

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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
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 · 2012: 1
FWCI
2.89
Type
journal article
Language
en
Open access
closed
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
  • Health Sciences › Medicine › Physiology › 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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