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Cited by 68Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Tau Aggregation in Alzheimer's Disease: What Role for Phosphorylation?

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Lippens, Guy, Sillen, Alain, Landrieu, Isabelle, Amniai, Laziza, Sibille, Nathalie, Barbier, Pascale, Leroy, Arnaud, Hanoulle, Xavier +1 more·2007·Prion
DOI 10.4161/pri.1.1.4055PMC PMC2633703
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Abstract

The crucial role of the neuronal Tau protein in microtubule stabilization and axonal transport suggests that too little or too much Tau might lead to neuronal dysfunction. The presence of a hyper phosphorylated but non aggregated molecule as a toxic species that might sequester normal Tau is discussed. We present recent in vitro results that might allow us to dissect the role of individual phosphorylation sites on its structure and function. We also discuss in this review the role of phosphorylation for the aggregation of the neuronal Tau protein, and compare it to the aggregation induced by external poly anions.

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  • Impairment of mitochondrial traffic is a feature of tauopathies.

    “Impairment of mitochondrial traffic is also a feature of tauopathies (Stokin et al., 2005;Lippens et al., 2007).”

    From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Lippens et al., 2007

    A passage labeled Abstract (page unavailable) says that tau deregulation can cause defects in axonal transport in Alzheimer’s disease and discusses transport of organelles. It does not specifically identify impaired mitochondrial traffic, so it supports the broader transport point but not the claim’s mitochondrial specificity. (LLM, conf=0.84)

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Cited by

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Authors
Lippens, G., Sillen, A., Landrieu, I., Amniai, L., Sibille, N., Barbier, P., Leroy, A., Hanoulle, X., & Wieruszeski, J.-M.
Affiliations
Centre National de la Recherche Scientifique (FR)
ORCID
Venue
Prion
Publisher
Informa UK Limited
Published
2007-01
Volume
1
Issue
1
Pages
21-25
ISSN
  • 1933-6896 (ISSN-L)
  • 1933-690X
DOI
10.4161/pri.1.1.4055
PMC
PMC2633703
OpenAlex
W1987975074
Cited by
68
References
5
Citations by year
2026: 3 · 2024: 4 · 2023: 8 · 2022: 4 · 2021: 6 · 2020: 8 · 2019: 9 · 2018: 6 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 4 · 2012: 3
FWCI
1.06
Type
journal article
Language
en
Open access
Locations
  • Prion (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL AMU (submittedVersion)
Funders
Agence Nationale de la Recherche
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
tau protein, tau aggregation, Alzheimer's disease, tau hyperphosphorylation, phosphorylation sites, microtubule stabilization, axonal transport, neuronal dysfunction, polyanions, protein aggregation
MeSH terms
Alzheimer Disease, Animals, Axons, Humans, Microtubules, Phosphorylation, Structure-Activity Relationship, tau Proteins, Protein Structure, Quaternary, Protein Transport

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