Microtubule lattice plasticity
Abstract
In classical microtubule dynamic instability, the dynamics of the built polymer depend only on the nucleotide state of its individual tubulin molecules. Recent work is overturning this view, pointing instead towards lattice plasticity, in which the fine-structure and mechanics of the microtubule lattice are emergent properties that depend not only on the nucleotide state of each tubulin, but also on the nucleotide states of its neighbours, on its and their isotypes, and on interacting proteins, drugs, local mechanical strain, post translational modifications, packing defects and solvent conditions. In lattice plasticity models, the microtubule is an allosteric molecular collective that integrates multiple mechanochemical inputs and responds adaptively by adjusting its conformation, stiffness and dynamics.
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The finding that stable cellular microtubules display expanded lattices directly supports the emerging model that microtubule lattice geometry functions as an additional cellular mechanism to guide protein binding specificity, on top of the previously established elements of the tubulin code.
“Our finding that stable cellular microtubules display expanded lattices now directly supports the emerging model that the microtubule lattice geometry functions as an additional cellular mechanism to guide protein binding specificity, on top of the previously established elements of the tubulin code”
From StableMARK-decorated microtubules in cells have expanded lattices (2025) · cites this paper as Cross, 2019
The different lattice spacings observed in the microtubule shaft likely play a role in microtubule stability, MAP binding, and motor protein kinetics.
“the different lattice spacings that we observe in the shaft of the microtubule likely play a role in microtubule stability, MAP binding, and motor protein kinetics, as has been previously postulated”
From StableMARK-decorated microtubules in cells have expanded lattices (2025) · cites this paper as Cross, 2019
Cites
Tubulin Posttranslational Modifications and Emerging Links to Human Disease
Magiera, M. M., Singh, P., Gadadhar, S., & Janke, C. (2018) · Cell · doi:10.1016/j.cell.2018.05.018 · Cited by 169 · see citing works
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StableMARK-decorated microtubules in cells have expanded lattices
de Jager, L., Jansen, K. I., Hoogebeen, R., Akhmanova, A., Kapitein, L. C., Förster, F., & Howes, S. C. (2025) · Journal of Cell Biology · doi:10.1083/jcb.202206143 · Cited by 25 · see citing works
- Authors
- Cross, R. A.
- Affiliations
- University of Warwick (GB)
- Corresponding author
- Cross, Robert A
- ORCID
- Cross, Robert A
- Venue
- Current Opinion in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 56
- Pages
- 88-93
- ISSN
- 0955-0674 (ISSN-L)
- OpenAlex
- W2899681969
- Cited by
- 43
- References
- 1
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 7 · 2021: 6 · 2020: 5 · 2019: 8
- FWCI
- 0.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Warwick Research Archive Portal (University of Warwick) (submittedVersion)
- Funders
- Wellcome Trust Senior Investigator Award (103895/Z/14/Z)
- 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 dynamic instability, microtubule mechanics, allosteric regulation, chemo-mechanical coupling, post-translational modification, packing defects, solvent conditions, microtubule-associated proteins
- MeSH terms
- Animals, Eukaryotic Cells, Humans, Microtubules, Molecular Conformation, Nucleotides, Tubulin, Polymerization
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