Cited by 625Alzheimer's disease research and treatmentsNeuroinflammation and Neurodegeneration MechanismsDementia and Cognitive Impairment Research

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Tau phosphorylation in neuronal cell function and dysfunction

Johnson, Gail V. W., Stoothoff, William H.·2004·Journal of Cell Science

DOI 10.1242/jcs.01558

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Abstract

Tau is a group of neuronal microtubule-associated proteins that are formed by alternative mRNA splicing and accumulate in neurofibrillary tangles in Alzheimer's disease (AD) brain. Tau plays a key role in regulating microtubule dynamics, axonal transport and neurite outgrowth, and all these functions of tau are modulated by site-specific phosphorylation. There is significant evidence that a disruption of normal phosphorylation events results in tau dysfunction in neurodegenerative diseases, such as AD, and is a contributing factor to the pathogenic processes. Indeed, the abnormal tau phosphorylation that occurs in neurodegenerative conditions not only results in a toxic loss of function (e.g. decreased microtubule binding) but probably also a toxic gain of function (e.g. increased tau-tau interactions). Although tau is phosphorylated in vitro by numerous protein kinases, how many of these actually phosphorylate tau in vivo is unclear. Identification of the protein kinases that phosphorylate tau in vivo in both physiological and pathological processes could provide potential therapeutic targets for the treatment of AD and other neurodegenerative diseases in which there is tau pathology.

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Authors: Johnson, G. V. W., & Stoothoff, W. H.
Affiliations: University of Alabama at Birmingham (US)
ORCID: Johnson, Gail V. W.
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2004-11-15
Volume: 117
Issue: 24
Pages: 5721-5729
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.01558
OpenAlex: W2118867129
Cited by: 624
References: 122
Citations by year: 2026: 10 · 2025: 25 · 2024: 27 · 2023: 53 · 2022: 36 · 2021: 38 · 2020: 47 · 2019: 33 · 2018: 41 · 2017: 31 · 2016: 32 · 2015: 19 · 2014: 32 · 2013: 29 · 2012: 29
FWCI: 1.32
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau phosphorylation, tau protein, Alzheimer's disease, neurofibrillary tangles, microtubule dynamics, axonal transport, neurite outgrowth, protein kinases, neurodegenerative diseases, therapeutic target
MeSH terms: Alzheimer Disease, Animals, Axons, Axonal Transport, Brain, Humans, Microtubules, Models, Biological, Neurons, Phosphorylation, RNA, Messenger, Neurofibrillary Tangles, tau Proteins, Alternative Splicing, Protein Structure, Tertiary, Neurodegenerative Diseases, Protein Isoforms

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Tau phosphorylation in neuronal cell function and dysfunction

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