Self-repair protects microtubules from destruction by molecular motors
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Abstract
Microtubule instability stems from the low energy of tubulin dimer interactions, which sets the growing polymer close to its disassembly conditions. Molecular motors use ATP hydrolysis to produce mechanical work and move on microtubules. This raises the possibility that the mechanical work produced by walking motors can break dimer interactions and trigger microtubule disassembly. We tested this hypothesis by studying the interplay between microtubules and moving molecular motors in vitro. Our results show that molecular motors can remove tubulin dimers from the lattice and rapidly destroy microtubules. We also found that dimer removal by motors was compensated for by the insertion of free tubulin dimers into the microtubule lattice. This self-repair mechanism allows microtubules to survive the damage induced by molecular motors as they move along their tracks. Our study reveals the existence of coupling between the motion of molecular motors and the renewal of the microtubule lattice.
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Such regional variation is consistent with previous studies and suggests that lattice conformation can be locally influenced by lattice-binding microtubule-associated proteins, post-translational modifications, mechanical stress, or repair processes.
“Such regional variation is consistent with previous studies58and suggest that lattice conformation can be locally influenced by lattice-binding microtuble-associated proteins (MAPs)59–61, post-translational modifications, mechanical stress50,51, or repair processes62–66.”
From Ghost Neuron preparation unlocks high-resolution structural mapping of intracellular architecture in axons (2026) · cites this paper as [62]
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Experimental — accuracy not yet measuredRecent evidence suggests that the microtubule lattice is not conformationally homogenous, but releases and incorporates new GTP-tubulin subunits in response to mechanical damage and repair.
“recent evidence suggests that the microtubule lattice is not conformationally homogenous, but rather releases and incorporates new GTP-tubulin subunits in response to mechanical damage and repair49.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [49]
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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
Mechanism and regulation of kinesin motors.
Yildiz, A. (2025) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-024-00780-6 · Cited by 88 · see citing works
MAP9/MAPH-9 supports axonemal microtubule doublets and modulates motor movement
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Bodakuntla, S., Marelli, J., Vasquez-Montes, V., Glauser, S., Biertümpfel, C., & Mizuno, N. (2026) · Nature Communications · doi:10.1038/s41467-026-77741-4
- Authors
- Triclin, S., Inoue, D., Gaillard, J., Htet, Z. M., DeSantis, M. E., Portran, D., Derivery, E., Aumeier, C., Schaedel, L., John, K., Leterrier, C., Reck-Peterson, S. L., Blanchoin, L., & Théry, M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- University of California San Diego (US)
- MRC Laboratory of Molecular Biology (GB)
- University of Geneva (CH)
- Corresponding author
- Blanchoin, Laurent
- Théry, Manuel
- ORCID
- Venue
- Nature Materials
- Published
- 2021-01-21
- Volume
- 20
- Issue
- 6
- Pages
- 883-891
- ISSN
- 1476-1122 (ISSN-L)
- 1476-4660
- PMC
- PMC7611741
- OpenAlex
- W3124900165
- Cited by
- 103
- References
- 3
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 9 · 2023: 18 · 2022: 30 · 2021: 12 · 2020: 6 · 2019: 4
- FWCI
- 8.97
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- Nature Materials (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion)
- PubMed Central (acceptedVersion, cc-by)
- HAL (submittedVersion, cc-by)
- HAL (submittedVersion)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- Howard Hughes Medical Institute
- Agence Nationale de la Recherche (ANR-17-EURE-0003, ANR-18-CE13-0001, ANR-10-LABX-0049)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- molecular motors, microtubule disassembly, microtubule lattice, ATP hydrolysis
- MeSH terms
- Microtubules, Models, Biological, Movement, Molecular Motor Proteins
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