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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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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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“Prior to initiating the screen, the robustness of the protocol was examined using two well characterized tau kinases, CDK5 (13) and GSK3 𝛃 (18), as well as GFP, the negative control.”
From An Unbiased Approach to Identifying Tau Kinases That Phosphorylate Tau at Sites Associated with Alzheimer Disease (2013) · cites this paper as [18]
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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)
- 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
- hybrid
- doi.org
- 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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