Role of tau protein in both physiological and pathological conditions
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Avila, Jesús, José J. Lucas, Mar Pérez, and Félix Hernández. Role of Tau Protein in Both Physiological and Pathological Conditions. Physiol Rev 84: 361–384, 2004; 10.1152/physrev.00024.2003.—The morphology of a neuron is determined by its cytoskeletal scaffolding. Thus proteins that associate with the principal cytoskeletal compo-nents such as the microtubules have a strong influence on both the morphology and physiology of neurons. Tau is a microtubule-associated protein that stabilizes neuronal microtubules under normal physiological conditions. However, in certain pathological situations, tau protein may undergo modifications, mainly through phosphorylation, that can result in the generation of aberrant aggregates that are toxic to neurons. This process occurs in a number of neurological disorders collectively known as tauopathies, the most commonly recognized of which is Alzheimer's disease. The purpose of this review is to define the role of tau protein under normal physiological conditions and to highlight the role of the protein in different tauopathies.
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In Alzheimer's disease, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments.
“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Avila et al., 2004
The section “Tau phosphorylation and development” states that tau can become hyperphosphorylated in Alzheimer’s disease. The section “Cellular and subcellular localization of tau protein” places phosphorylated tau in somatodendritic compartments in developing neurons, but does not establish that tau mislocalizes there in Alzheimer’s disease. Page numbers were not available in our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredUnder normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules.
“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Avila et al., 2004
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“This is because, as is detailed in a 2004 paper by Avila and colleagues in Physiology Reviews (Avila et al., 2004), these proteins are implicated in several different diseases.”
MethodAnti-Correlated Cerebrospinal Fluid Biomarker Trajectories in Preclinical Alzheimer’s Disease
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- Authors
- AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F.
- Affiliations
- Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM), Facultad de Ciencias, Campus de Cantoblanco, Madrid, Spain
- Consejo Superior de Investigaciones Científicas (ES)
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2004-04
- Volume
- 84
- Issue
- 2
- Pages
- 361-384
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2164136371
- Cited by
- 1,005
- References
- 18
- Citations by year
- 2026: 55 · 2025: 70 · 2024: 74 · 2023: 78 · 2022: 55 · 2021: 55 · 2020: 61 · 2019: 30 · 2018: 43 · 2017: 40 · 2016: 49 · 2015: 54 · 2014: 49 · 2013: 39 · 2012: 40
- FWCI
- 3.51
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Locations
- Physiological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Biblos-e Archivo (Universidad Autónoma de Madrid) (submittedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Hispana (submittedVersion)
- Funders
- Eli Lilly and Company
- Comunidad de Madrid
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, microtubule stabilization, tau phosphorylation, tauopathy, Alzheimer's disease, neuronal cytoskeleton, microtubule-associated proteins, neurodegeneration, tau aggregates
- MeSH terms
- Animals, Disease Models, Animal, Humans, Microtubules, Neurons, Protein Processing, Post-Translational, tau Proteins, Tauopathies
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