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Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding
Abstract
Tau protein, a component of Alzheimer paired helical filaments, can be phosphorylated by several kinases. Of particular interest is the phosphorylation at Ser/Thr-Pro motifs because the resulting state of tau is similar to that found in Alzheimer's disease, as judged by its immunoreactivity. This state can be mimicked by a brain extract kinase activity and by MAP kinase. We have now studied the effect of these modes of phosphorylation on the interaction between tau and microtubules. Although MAP kinase efficiently phosphorylates many Ser/Thr-Pro motifs of tau, its effect on microtubule binding is only moderate. By contrast, phosphorylation of a single residue, Ser262, has a major effect on binding. Ser262 is not phosphorylated by MAP kinase or other proline-directed kinases, but is phosphorylated by a 35/41 kd kinase in brain, whose purification is described.
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In the citing paper
“Tau hyperphosphorylation reduces its ability to stabilize microtubules [3–5]”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [4]
In the citing paper
“In addition, phosphorylation of Tau reduces its ability to bind and stabilize microtubules [3–5].”
From Elevated SGK1 increases Tau phosphorylation and microtubule instability in Alzheimer’s patient-derived cortical neurons (2026) · cites this paper as [4]
In the citing paper
“Phosphorylation of serine residues at KXGS motifs in the repeat domain of Tau, such as S262, strongly reduce the affinity of Tau for microtubules75.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [75]
In the citing paper
“While our as well as previous biophysical studies demonstrated that phosphorylation at the KXGS motifs decreases the affinity of Tau for both microtubules and F-actin, cellular studies showed that phosphorylation of the KXGS motifs cause MAP2 and Tau to localize to the actin cytoskeleton9.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [75]
In the citing paper
“Tau phosphorylation at these sites decreases the protein’s affinity toward microtubules in vitro, in cultured cells, transgenic Drosophila, and transgenic mice [18, 19, 25–27, 50–52].”
In the citing paper
“and is often found detached from microtubules in vitro and in cultured cells [51, 90].”
In the citing paper
“Ser262 and Ser356 are located in the microtubule-binding domain, and phosphorylation at these sites decreases tau binding to microtubules [18, 19, 25, 26, 50, 51].”
In the citing paper
“Phosphorylation of tau negatively influences its ability to bind microtubules [25–27, 51, 52].”
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Metadata
- Authors
- Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E.
- Affiliations
- Deutsches Elektronen-Synchrotron DESY (DE)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1993-07
- Volume
- 11
- Issue
- 1
- Pages
- 153-163
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2039468514
- Cited by
- 796
- References
- 3
- Citations by year
- 2026: 15 · 2025: 22 · 2024: 26 · 2023: 24 · 2022: 25 · 2021: 22 · 2020: 36 · 2019: 24 · 2018: 28 · 2017: 27 · 2016: 20 · 2015: 23 · 2014: 30 · 2013: 28 · 2012: 28
- FWCI
- 19.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion)
- 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 › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- tau protein, microtubule binding, Alzheimer's disease, paired helical filaments, mitogen-activated protein kinase, proline-directed kinases, tau phosphorylation
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Animals, Antibodies, Brain, Humans, Microtubules, Molecular Sequence Data, Peptide Fragments, Phosphorylation, Phosphotransferases, Protein Kinases, tau Proteins, Calcium-Calmodulin-Dependent Protein Kinases
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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