Microtubules gate tau condensation to spatially regulate microtubule functions
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Abstract
Tau is an abundant microtubule-associated protein in neurons. Tau aggregation into insoluble fibrils is a hallmark of Alzheimer's disease and other types of dementia 1, yet the physiological state of tau molecules within cells remains unclear. Using single-molecule imaging, we directly observe that the microtubule lattice regulates reversible tau self-association, leading to localized, dynamic condensation of tau molecules on the microtubule surface. Tau condensates form selectively permissible barriers, spatially regulating the activity of microtubule-severing enzymes and the movement of molecular motors through their boundaries. We propose that reversible self-association of tau molecules, gated by the microtubule lattice, is an important mechanism of the biological functions of tau, and that oligomerization of tau is a common property shared between the physiological and disease-associated forms of the molecule.
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The microtubule-binding repeats, together with the proline-rich region and the C-terminus, define the minimal domains required for cooperative binding.
“The microtubule-binding repeats, together with the proline-rich region and the C-terminus, define the minimal domains required for cooperative binding (Tan et al., 2019).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
In the tau-domain mapping passage (Fig. 3a–d; page unavailable), adding the proline-rich region and C-terminal pseudo-repeat to the microtubule-binding domain restores incorporation into tau condensates. A separate passage (Fig. 2c–d; page unavailable) attributes condensate cohesiveness to cooperative interactions between tau molecules. The paper does not establish that these three regions are the minimal domains required for cooperative binding. (LLM, conf=0.84)
Experimental — accuracy not yet measuredEnvelope formation is sensitive to the intramolecular lattice spacing between α and β tubulin.
“Envelope formation is sensitive to the intramolecular lattice spacing between α and β tubulin.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
The passage labelled Abstract (page not given) reports that tau condensates form on some microtubule lattices but not others, and hypothesizes that spacing affects condensation. It specifies spacing between tubulin dimers, not spacing between α- and β-tubulin within a dimer; it also presents the spacing mechanism as a hypothesis rather than an established result. (LLM, conf=0.88)
Experimental — accuracy not yet measuredTau does not form envelopes on GMPCPP-polymerized microtubules, but readily forms envelopes on compacted GDP-lattices or reversibly expanded taxol-lattices.
“Tau does not form envelopes on GMPCPP-polymerized microtubules, which are irreversibly expanded, mimicking the GTP-state, but readily forms envelopes on compacted GDP-lattices or reversibly expanded taxol-lattices”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
The paper’s passage labeled Abstract (page unavailable) reports that tau condensates formed on taxol-stabilized and native GDP microtubule lattices, but not on GMP-CPP lattices. It also reports that GMP-CPP lattices are expanded relative to GDP lattices. Our copy does not establish the sentence’s further descriptions of GMP-CPP expansion as irreversible or taxol-lattice expansion as reversible. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThese regions together with the microtubule-binding repeats comprise the minimal domains required for cooperative binding.
“which together with the microtubule-binding repeats, comprise the minimal domains required for cooperative binding”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
The domain-truncation passage (section labeled Abstract; page unavailable) shows that adding the proline-rich and pseudo-repeat regions to the microtubule-binding domain restores incorporation into tau condensates to near full-length levels. The paper also describes cooperative interactions between tau molecules within condensates, but it does not establish that these are the minimal domains required for cooperative binding: a construct lacking the microtubule-binding domain also incorporated, though weakly. (LLM, conf=0.84)
Experimental — accuracy not yet measuredThe proline-rich region and C-terminal pseudo-repeat domain of tau regulate its cooperative interactions with microtubules.
“the proline-rich region and C-terminal pseudo-repeat domain of tau regulate its cooperative interactions with microtubules”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
The passage discussing Fig. 3 reports that adding the proline-rich and C-terminal pseudo-repeat regions restores tau incorporation into condensates on microtubules. The passage discussing Fig. 2 describes cooperative interactions between tau molecules within those condensates. It does not establish that both regions regulate cooperative tau–microtubule interactions specifically; it distinguishes tau self-association from tau’s affinity for microtubules. (LLM, conf=0.82)
Experimental — accuracy not yet measured
Tau molecules inside envelopes do not diffuse but remain stationary.
“since tau molecules inside envelopes do not diffuse, but remain stationary9,28.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
The passage describing single-molecule behavior says tau becomes statically bound at condensate boundaries, supporting the stationary characterization. But it also reports a nonzero diffusion coefficient within condensates (4×10−4 µm²/s), so the absolute claim that molecules inside them do not diffuse overstates the result. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe MAP2c level outside of envelopes was identical to that on GMPCPP-lattice microtubules, similar to tau.
“Quantification of MAP intensity on both types of lattices revealed that the MAP2c level outside of the envelopes was identical to that on GMPCPP-lattice microtubules, similar to tau9.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
The passage discussing Fig. 1i–j (page unavailable) reports diffuse tau binding on both taxol-stabilized and GMP-CPP microtubules, with condensates forming only on the former. This supports the broad comparison to tau, but the cited paper does not state that tau intensity outside condensates was identical to its intensity on GMP-CPP microtubules. The MAP2c measurement is the citing authors’ own result, not a result attributed to this source. (LLM, conf=0.78)
Experimental — accuracy not yet measured1,6-Hexanediol disrupts phase separated systems in a variety of biological contexts.
“Tau envelopes are sensitive to the aliphatic alcohol 1,6-hexanediol (1,6-HD), a compound that disrupts phase separated systems in a variety of biological contexts9”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
The paper’s Abstract (page not available in our copy) reports that 1,6-hexanediol rapidly dissolved microtubule-bound tau condensates and notes that it has been shown to dissolve tau droplets formed by liquid–liquid phase separation. This supports the effect on tau systems, but the paper does not establish that it disrupts phase-separated systems across a variety of biological contexts. (LLM, conf=0.86)
Experimental — accuracy not yet measuredDiscontinuous patterning of tau along microtubules, consistent with envelopes, was observed in live non-neuronal U-2 OS cells following taxol treatment or elevated pH, and by immunofluorescence in fixed hippocampal neurons.
“Discontinuous patterning of tau along microtubules, consistent with envelopes, was also observed in live, non-neuronal U-2 OS cells following taxol treatment (Siahaan et al., 2022) or with elevated pH (Siahaan et al., 2026), and by immunofluorescence staining in fixed hippocampal neurons (Tan et al., 2019).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Tan et al., 2019
Tau was highly co-enriched within tau envelopes.
“As expected9, tau was highly co-enriched within tau envelopes”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
Tau envelopes form on GDP microtubule lattices but do not form on GMPCPP-stabilized microtubules.
“Previously, we observed that tau envelopes form on GDP microtubule lattices but do not form on microtubules stabilized with GMPCPP9.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
MAP2c envelopes dissolved when exposed to 1,6-hexanediol, but the diffusive fraction of MAP2c molecules remained unchanged.
“Similar to tau9, MAP2c envelopes dissolved when exposed to 1,6-HD, but the diffusive fraction of MAP2c molecules remained unchanged”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
Kinesin binding expands the microtubule lattice, suggesting that exclusive binding may arise from competition for an expanded versus compacted lattice.
“Apart from steric clashes between tau and kinesin9,41, kinesin binding expands the microtubule lattice4,6 suggesting that exclusive binding may arise from competition for an expanded versus compacted lattice.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
During taxol-driven extension of the native compacted microtubule lattice, tau signal disappeared from microtubules in patterns resembling disassembly of tau envelopes in vitro.
“we found that the tau signal disappeared from the microtubules in patterns that resembled the disassembly of tau envelopes in vitro9,28.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [9]
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Cited by
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A combinatorial MAP code dictates polarized microtubule transport
Monroy, B. Y., Tan, T. C., Oclaman, J. M., Han, J. S., Simó, S., Niwa, S., Nowakowski, D. W., McKenney, R. J., & Ori-McKenney, K. M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.01.029 · Cited by 157 · see citing works
Self-citationBaas, P. W., & Qiang, L. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.02.007 · Cited by 123 · see citing works
Microtubule lattice spacing governs cohesive envelope formation of tau family proteins
Siahaan, V., Tan, R., Humhalova, T., Libusova, L., Lacey, S. E., Tan, T., Dacy, M., Ori-McKenney, K. M., McKenney, R. J., Braun, M., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01096-2 · Cited by 94 · see citing works
Self-citationModeling late-onset Alzheimer’s disease neuropathology via direct neuronal reprogramming
Sun, Z., Kwon, J.-S., Ren, Y., Chen, S., Walker, C. K., Lu, X., Cates, K., Karahan, H., Sviben, S., Fitzpatrick, J. A. J., et al. (2024) · Science · doi:10.1126/science.adl2992 · Cited by 77 · see citing works
“Both ADAD and HC neurites displayed p-tau signals, mirroring the tau island patterns observed in primary neurons (20, 38, 39) (Fig.”
Capano, L. S., Sato, C., Ficulle, E., Yu, A., Horie, K., Kwon, J.-S., Burbach, K. F., Barthélemy, N. R., Fox, S. G., Karch, C. M., et al. (2022) · Cell Stem Cell · doi:10.1016/j.stem.2022.04.018 · Cited by 65 · see citing works
Liquid − liquid phase separation of tau: Driving forces, regulation, and biological implications
Li, P., Chen, J., Wang, X., Su, Z., Gao, M., & Huang, Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106167 · Cited by 30 · see citing works
Beaudet, D., Berger, C. L., & Hendricks, A. G. (2026) · eLife · doi:10.7554/elife.110011
- Authors
- Tan, R., Lam, A. J., Tan, T., Han, J., Nowakowski, D. W., Vershinin, M., Simó, S., Ori-McKenney, K. M., & McKenney, R. J.
- Affiliations
- University of California, Davis (US)
- University of Utah (US)
- Corresponding author
- Ori-McKenney, Kassandra M.
- McKenney, Richard J.
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2019-09
- Volume
- 21
- Issue
- 9
- Pages
- 1078-1085
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC6748660
- OpenAlex
- W2971541306
- Cited by
- 231
- References
- 3
- Citations by year
- 2026: 38 · 2025: 28 · 2024: 24 · 2023: 38 · 2022: 26 · 2021: 35 · 2020: 32 · 2019: 10
- FWCI
- 17.25
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Nature Cell Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- NSF | BIO | Division of Molecular and Cellular Biosciences (ENG-1563280)
- Pew Charitable Trusts (A19-0406)
- U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (R00NS089428)
- U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (R35GM124889)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- tau protein, microtubule lattice, tau oligomerization, molecular motors, Alzheimer's disease, tau aggregation, single-molecule imaging
- MeSH terms
- Spastin, Animals, Microtubule-Associated Proteins, Microtubules, Neurons, Swine, tau Proteins, Mice, Neuroimaging
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