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Mechanistic basis of temperature-adaptation in microtubule dynamics across frog species
Open accessPreprint — published as 10.1016/j.cub.2024.12.022 · Paper page
Abstract
SUMMARY: Cellular processes are remarkably effective across diverse temperature ranges, even with highly conserved proteins. In the context of the microtubule cytoskeleton, which is critically involved in a wide range of cellular activities, this is particularly striking as tubulin is one of the most conserved proteins while microtubule dynamic instability is highly temperature sensitive. We thus lack a mechanistic framework that links functional adaptability with environmental pressures. Here, we leverage the diversity of natural tubulin variants from three closely related frog species that live at different temperatures: we combine in vitro reconstitution assays, quantitative biochemistry, and cryogenic electron microscopy to show how a small number of primary sequence changes influences the energy landscape of tubulin interactions and thereby mediates cold-adaptation and microtubule stability. This study thus broadens our conceptual framework for understanding microtubule dynamics and provides insights into how conserved cellular processes are tailored to different ecological niches.
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Metadata
- Authors
- Troman, L., de Gaulejac, E., Biswas, A., Stiens, J., Kuropka, B., Moores, C., & Reber, S.
- Affiliations
- Institute of Structural and Molecular Biology (GB)
- Humboldt-Universität zu Berlin (DE)
- Marine Biological Laboratory (US)
- Freie Universität Berlin (DE)
- Berliner Hochschule für Technik (DE)
- Corresponding author
- Moores, Carolyn
- Reber, Simone
- Venue
- Current Biology
- Publisher
- openRxiv
- Published
- 2024-07-29
- Volume
- 35
- Issue
- 3
- Pages
- 612-628.e6
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W4406235478
- Cited by
- 11
- References
- 1
- Citations by year
- 2026: 6 · 2025: 5
- FWCI
- 5.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- BIROn (Birkbeck, University of London) (acceptedVersion)
- Open Access Server of the Woods Hole Scientific Community (Woods Hole Scientific Community) (submittedVersion, cc-by-nc)
- Funders
- Wellcome Trust (202679/Z/16/Z, 206166/Z/17/Z)
- Deutsche Forschungsgemeinschaft
- Max-Planck-Gesellschaft
- Medical Research Council (MR/Y000633/1, MR/R00352/1, MR/R000352/1)
- Medical Research Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Keywords
- microtubule dynamics, thermal adaptation, tubulin, cold adaptation, frogs, microtubule structure, cytoskeleton
- MeSH terms
- Animals, Microtubules, Temperature, Tubulin, Cryoelectron Microscopy
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