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Cited by 226Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments

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Maas, Thorsten, Eidenmüller, Jochen, Brandt, Roland·2000·Journal of Biological Chemistry
DOI 10.1074/jbc.m000389200
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Abstract

The axonal microtubule-associated phosphoprotein tau interacts with neural plasma membrane (PM) components during neuronal development (Brandt, R., Léger, J., and Lee, G. (1995) J. Cell Biol. 131, 1327-1340). To analyze the mechanism and potential regulation of tau's PM association, a method was developed to isolate PM-associated tau using microsphere separation of surface-biotinylated cells. We show that tau's PM association requires an intact membrane cortex and that PM-associated tau and cytosolic tau are differentially phosphorylated at sites detected by several Alzheimer's disease (AD) diagnostic antibodies (Ser(199)/Ser(202), Thr(231), and Ser(396)/Ser(404)). In polar neurons, the association of endogenous tau phosphoisoforms with the membrane cortex correlates with an enrichment in the axonal compartment. To test for a direct effect of AD-specific tau modifications in determining tau's interactions, a phosphomutant that simulates an AD-like hyperphosphorylation of tau was produced by site-directed mutagenesis of Ser/Thr residues to negatively charged amino acids (Glu). These mutations completely abolish tau's association with the membrane cortex; however, the construct retains its capability to bind to microtubules. The data suggest that a loss of tau's association with the membrane cortex as a result of phosphorylation at sites that are modified during disease contributes to somatodendritic tau accumulation, axonal microtubule disintegration, and neuronal death characteristic for AD.

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  1. Prickett, 1989, BioTechniques, 7, 580

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Metadata

Authors
Maas, T., Eidenmüller, J., & Brandt, R.
Affiliations
Heidelberg University (DE)
Corresponding author
Brandt, Roland
ORCID
Brandt, Roland
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-05
Volume
275
Issue
21
Pages
15733-15740
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.m000389200
OpenAlex
W2061655823
Cited by
226
References
50
Citations by year
2026: 2 · 2025: 4 · 2024: 2 · 2023: 6 · 2022: 9 · 2021: 9 · 2020: 9 · 2019: 10 · 2018: 10 · 2017: 14 · 2016: 7 · 2015: 17 · 2014: 18 · 2013: 11 · 2012: 14
FWCI
5.22
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
Deutsche Forschungsgemeinschaft (SFB 31 7)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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 phosphorylation, paired helical filaments, Alzheimer's disease, plasma membrane association, axonal microtubules, tau hyperphosphorylation, neuronal cell death
MeSH terms
Actins, Alzheimer Disease, Animals, Cell Membrane, Cytosol, Immunohistochemistry, Microscopy, Electron, Microspheres, Microtubules, Neurons, Phosphorylation, Protein Binding, Transfection, Mutagenesis, Site-Directed, PC12 Cells, tau Proteins, Microscopy, Confocal, Okadaic Acid, Biotinylation, Rats

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