The Structure and Dynamics of C. elegans Tubulin Reveals the Mechanistic Basis of Microtubule Growth
Open accessAbstract
The dynamic instability of microtubules is a conserved and fundamental mechanism in eukaryotes. Yet microtubules from different species diverge in their growth rates, lattice structures, and responses to GTP hydrolysis. Therefore, we do not know what limits microtubule growth, what determines microtubule structure, or whether the mechanisms of dynamic instability are universal. Here, we studied microtubules from the nematode C. elegans, which have strikingly fast growth rates and non-canonical lattices in vivo. Using a reconstitution approach, we discovered that C. elegans microtubules combine intrinsically fast growth with very frequent catastrophes. We solved the structure of C. elegans microtubules to 4.8 Å and discovered sequence divergence in the lateral contact loops, one of which is ordered in C. elegans but unresolved in other species. We provide direct evidence that C. elegans tubulin has a higher free energy in solution and propose a model wherein the ordering of lateral contact loops activates tubulin for growth.
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In non-mammalian species, microtubule lattice compaction does not appear to be directly coupled to GTP hydrolysis.
“in non-mammalian species, microtubule lattice compaction does not appear to be directly coupled to GTP hydrolysis47,48.”
From Microtubule lattice spacing governs cohesive envelope formation of tau family proteins (2022) · cites this paper as [48]
The available copy yields only a corrupted table of contents, with no readable passage addressing whether microtubule lattice compaction is coupled to GTP hydrolysis. Searches for “lattice compaction GTP hydrolysis,” “compaction,” and an uncoupled-lattice paraphrase found no decisive text. (LLM, conf=0.72)
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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
Khan, N., Pelletier, D., McAlear, T. S., Croteau, N., Veyron, S., Bayne, A. N., Black, C., Ichikawa, M., Khalifa, A. A. Z., Chaaban, S., et al. (2021) · Structure · doi:10.1016/j.str.2021.01.001 · Cited by 24 · see citing works
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- Authors
- Chaaban, S., Jariwala, S., Hsu, C.-T., Redemann, S., Kollman, J. M., Müller-Reichert, T., Sept, D., Bui, K. H., & Brouhard, G. J.
- Affiliations
- University of Michigan (US)
- University of Virginia (US)
- McGill University (CA)
- Corresponding author
- Brouhard, Gary J.
- ORCID
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2018-10
- Volume
- 47
- Issue
- 2
- Pages
- 191-204.e8
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W2892377120
- Cited by
- 83
- References
- 0
- Citations by year
- 2026: 8 · 2025: 9 · 2024: 9 · 2023: 6 · 2022: 13 · 2021: 14 · 2020: 11 · 2019: 10 · 2018: 3
- FWCI
- 5.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Developmental Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- McGill University
- Canadian Institutes of Health Research (MOP-130376, MOP-137055, PJT-148702)
- German Research Foundation (MU 1423/8-1)
- Natural Sciences and Engineering Research Council of Canada (69462, 03791)
- Canadian Institute for Advanced Research
- Fonds de recherche du Québec—Nature et technologies (191128)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- microtubule dynamic instability, microtubule growth, tubulin, Caenorhabditis elegans, catastrophe, GTP hydrolysis
- MeSH terms
- Animals, Guanosine Triphosphate, Microtubules, Models, Molecular, Structure-Activity Relationship, Tubulin, Caenorhabditis elegans, Caenorhabditis elegans Proteins
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