Self-repair promotes microtubule rescue
Open accessAbstract
The dynamic instability of microtubules is characterized by slow growth phases stochastically interrupted by rapid depolymerizations called catastrophes. Rescue events can arrest the depolymerization and restore microtubule elongation. However, the origin of these rescue events remains unexplained. Here we show that microtubule lattice self-repair, in structurally damaged sites, is responsible for the rescue of microtubule growth. Tubulin photo-conversion in cells revealed that free tubulin dimers can incorporate along the shafts of microtubules, especially in regions where microtubules cross each other, form bundles or become bent due to mechanical constraints. These incorporation sites appeared to act as effective rescue sites ensuring microtubule rejuvenation. By securing damaged microtubule growth, the self-repair process supports a mechanosensitive growth by specifically promoting microtubule assembly in regions where they are subjected to physical constraints.
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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 [64]
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- Authors
- Aumeier, C., Schaedel, L., Gaillard, J., John, K., Blanchoin, L., & Théry, M.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Blanchoin, Laurent
- Théry, Manuel
- Venue
- Nature Cell Biology
- Published
- 2016-09-12
- Volume
- 18
- Issue
- 10
- Pages
- 1054-1064
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC5045721
- OpenAlex
- W2519267297
- Cited by
- 181
- References
- 1
- Citations by year
- 2026: 13 · 2025: 8 · 2024: 16 · 2023: 25 · 2022: 20 · 2021: 17 · 2020: 18 · 2019: 25 · 2018: 26 · 2017: 7 · 2016: 6
- FWCI
- 12.19
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- Funders
- Agence Nationale de la Recherche (ANR-12-BSV5-0014)
- 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
- microtubule rescue, microtubule dynamic instability, microtubule catastrophe, microtubule bundling, microtubule bending, microtubule assembly
- MeSH terms
- Animals, Cell Membrane, Cells, Cultured, Microtubule-Associated Proteins, Microtubules, Photolysis, Tubulin, Rats, Focal Adhesion Kinase 1
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