Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
Open accessAbstract
Significance: Tau is an important microtubule-associated protein. Although the structure–function relationship of Tau has been intensively studied for many years primarily by molecular biology and biochemical approaches, little is still known about the molecular mechanisms by which Tau interacts with microtubules and promotes microtubule assembly. Here, we provide detailed insight into the Tau–microtubule association by using NMR spectroscopy and mass spectrometry. We show that Tau binds to microtubules by using small groups of residues, which are important for pathological aggregation of Tau. We further show that Tau stabilizes a straight protofilament conformation by binding to a hydrophobic pocket in between tubulin heterodimers. Our work is thus relevant to normal Tau action development and in Tau-related neurodegenerative diseases.
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Tau residues 168-185, 224-237, 245-253, 269-284, 300-313, and 375-398 bind to microtubules at the interface between tubulin heterodimers.
“We previously showed that the Tau residues 168–185, 224–237, 245–253, 269–284, 300–313, and 375–398 bind to microtubules at the interface between tubulin heterodimers (Fig. 5b)72.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [72]
The Significance passage (p. 2) identifies residues 224–237 and 245–253 as microtubule-binding motifs, and the paper states that Tau binds at the interface between tubulin heterodimers (p. 1). But it gives the other measured motifs as 275–284 and 300–317, not 269–284 and 300–313. The available passages do not identify 168–185 or 375–398 as binding motifs at that precise interface. (LLM, conf=0.86)
Experimental — accuracy not yet measuredTau is a microtubule-associated protein that stabilizes microtubules by interacting with tubulin heterodimers, supporting axonal structure and neuronal morphology.
“The microtubule-associated protein tau (MAPT) was first identified as a key regulator of microtubule stability and assembly [1]. Tau stabilizes microtubules by interacting with tubulin heterodimers, thereby supporting axonal structure and maintaining neuronal morphology [2–4].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [4]
Tau promotes the polymerization and stability of microtubules.
“As a microtubule binding component, tau promotes the polymerization and stability of microtubules [119–121].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [120]
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- Authors
- Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M.
- Affiliations
- Max Planck Society (DE)
- German Center for Neurodegenerative Diseases (DE)
- Deutsches Zentrum für Neurodegenerative Erkrankungen, Ludwig-Erhard-Allee 2, Bonn, Germany;
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2015-06
- Volume
- 112
- Issue
- 24
- Pages
- 7501-7506
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC4475932
- OpenAlex
- W1568323816
- Cited by
- 524
- References
- 57
- Citations by year
- 2026: 29 · 2025: 48 · 2024: 50 · 2023: 61 · 2022: 53 · 2021: 55 · 2020: 49 · 2019: 61 · 2018: 53 · 2017: 29 · 2016: 26 · 2015: 10
- FWCI
- 28.98
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DZNE Pub (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (ZW 71/8-1)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, microtubule stabilization, tubulin heterodimers, microtubule-binding site, microtubule-associated proteins, tau aggregation, Alzheimer's disease, protein flexibility, microtubule assembly, cell morphology
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Binding, Competitive, Humans, Microtubules, Models, Molecular, Protein Binding, Swine, Tubulin, Vinblastine, tau Proteins, Nuclear Magnetic Resonance, Biomolecular, Protein Isoforms, Protein Structure, Quaternary, Protein Interaction Domains and Motifs, Protein Multimerization, Biophysical Phenomena
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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