The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Dynamic association of tau with neuronal membranes is regulated by phosphorylation
Abstract
Tau is an abundant cytosolic protein which regulates cytoskeletal stability by associating with microtubules in a phosphorylation-dependent manner. We have found a significant proportion of tau is located in the membrane fraction of rat cortical neurons and is dephosphorylated, at least at Tau-1 (Ser199/Ser202), AT8 (Ser199/Ser202/Thr205) and PHF-1 (Ser396/Ser404) epitopes. Inhibition of tau kinases casein kinase 1 (CK1) or glycogen synthase kinase-3 decreased tau phosphorylation and significantly increased amounts of tau in the membrane fraction. Mutation of serine/threonine residues to glutamate to mimic phosphorylation in the N-terminal, but not C-terminal, region of tau prevented its membrane localization in transfected cells, demonstrating that the phosphorylation state of tau directly impacts its localization. Inhibiting CK1 in neurons lacking the tyrosine kinase fyn also induced tau dephosphorylation but did not affect its membrane association. Furthermore, inhibition of CK1 increased binding of neuronal tau to the fyn-SH3 domain. We conclude that trafficking of tau between the cytosol and the neuronal membrane is dynamically regulated by tau phosphorylation through a mechanism dependent on fyn expression.
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“Apart from its effects on microtubule binding, phosphorylation can alter tau subcellular localization to dendritic spines (127) or can alter its affinity for the plasma membrane (128), thereby causing alterations in synaptic function (127,129).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [128]
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Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
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GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
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Self-citationAltered expression of synaptic proteins occurs early during progression of Alzheimer's disease
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Mechanisms of tau-induced neurodegeneration
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Tau phosphorylation in neuronal cell function and dysfunction
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Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
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Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Self-citationPhysiological release of endogenous tau is stimulated by neuronal activity
Pooler, A. M., Phillips, E. C., Lau, D. H. W., Noble, W., & Hanger, D. P. (2013) · The EMBO Reports · doi:10.1038/embor.2013.15 · Cited by 642
Self-citationArendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609
The importance of tau phosphorylation for neurodegenerative diseases
Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475
Self-citationStructure and Pathology of Tau Protein in Alzheimer Disease
Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řípová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 526
Metadata
- Authors
- Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P.
- Affiliations
- King's College London (GB)
- GlaxoSmithKline (United Kingdom) (GB)
- Corresponding author
- Pooler, Amy M.
- Venue
- Neurobiology of Aging
- Publisher
- Elsevier BV
- Published
- 2012-02
- Volume
- 33
- Issue
- 2
- Pages
- 431.e27-431.e38
- ISSN
- 0197-4580 (ISSN-L)
- OpenAlex
- W2011813094
- Cited by
- 148
- References
- 46
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 8 · 2022: 8 · 2021: 15 · 2020: 10 · 2019: 8 · 2018: 11 · 2017: 16 · 2016: 10 · 2015: 15 · 2014: 12 · 2013: 16 · 2012: 5
- FWCI
- 8.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neurobiology of Aging (publishedVersion)
- PubMed (publishedVersion)
- Research Portal (King's College London) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau protein, tau phosphorylation, tau dephosphorylation, casein kinase 1, glycogen synthase kinase-3, Fyn tyrosine kinase, Fyn SH3 domain, cortical neurons, microtubule stabilization
- MeSH terms
- Animals, Animals, Newborn, Cell Membrane, Cells, Cultured, Neurons, tau Proteins, Rats, Sprague-Dawley, Glycogen Synthase Kinase 3, Casein Kinase I, Rats
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