Biochemistry of Tau in Alzheimer’s disease and related neurological disorders
Abstract
Microtubule-associated Tau proteins belong to a family of factors that polymerize tubulin dimers and stabilize microtubules. Tau is strongly expressed in neurons, localized in the axon and is essential for neuronal plasticity and network. From the very beginning of Tau discovery, proteomics methods have been essential to the knowledge of Tau biochemistry and biology. In this review, we have summarized the main contributions of several proteomic methods in the understanding of Tau, including expression, post-translational modifications and structure, in both physiological and pathophysiological aspects. Finally, recent advances in proteomics technology are essential to develop further therapeutic targets and early predictive and discriminative diagnostic assays for Alzheimer's disease and related disorders.
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More than 20 Ser/Thr kinases have been shown to phosphorylate tau in vitro.
“more than 20 Ser/Thr kinases have been shown to phosphorylate tau in vitro .”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [5]
Numerous tau phosphorylation sites are associated with tau dysfunction and neurodegeneration.
“Numerous tau phosphorylation sites are associated with tau dysfunction and neurodegeneration (5, 6).”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [5]
In vitro findings that numerous kinases phosphorylate tau may not reflect the situation in a cellular system.
“however, these may not reflect the situation in a cellular system.”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [5]
It remains uncertain which kinases actually phosphorylate tau in vivo.
“However, there is still uncertainty about which of these kinases actually phosphorylate tau in vivo (for reviews, see Refs. 5 and 6).”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [5]
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References 161 · Cited by 300
- Authors
- Sergeant, N., Bretteville, A., Hamdane, M., Caillet-Boudin, M.-L., Grognet, P., Bombois, S., Blum, D., Delacourte, A., Pasquier, F., Vanmechelen, E., Schraen-Maschke, S., & Buée, L.
- Affiliations
- Inserm (FR)
- Fujirebio (Belgium) (BE)
- Université de Lille (FR)
- ORCID
- Venue
- Expert Review of Proteomics
- Publisher
- Informa UK Limited
- Published
- 2008-04
- Volume
- 5
- Issue
- 2
- Pages
- 207-224
- ISSN
- 1478-9450 (ISSN-L)
- 1744-8387
- OpenAlex
- W2096278785
- Cited by
- 300
- References
- 161
- Citations by year
- 2026: 9 · 2025: 10 · 2024: 16 · 2023: 8 · 2022: 22 · 2021: 21 · 2020: 25 · 2019: 20 · 2018: 16 · 2017: 17 · 2016: 14 · 2015: 18 · 2014: 26 · 2013: 16 · 2012: 23
- FWCI
- 8.75
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Expert Review of Proteomics (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, Alzheimer's disease, tauopathy, microtubule stabilization, microtubule assembly, post-translational modification, proteomics, therapeutic target, diagnostic biomarkers, neuroplasticity
- MeSH terms
- Alzheimer Disease, Humans, Nervous System Diseases, Protein Processing, Post-Translational, tau Proteins, Protein Isoforms
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