ArticleNature communications2022
The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 39 citations in OpenAlex.
- Post-Translational Modifications of Tubulin in Oocyte Maturation and Female Infertility.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Article
- Enhanced processivity and collective force production of kinesin-1 at low radial forces.eLife · 2026Article
- Microtubule lattice conformation and integrity regulate α-tubulin acetylation.Communications biology · 2026Article
- Kinesin-Induced Buckling Reveals the Limits of Microtubule Self-Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Enhanced Processivity and Collective Force Production of Kinesin-1 at Low Radial Forces.bioRxiv : the preprint server for biology · 2025Article
- WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation.The Journal of cell biology · 2025Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Continuous self-repair protects vimentin intermediate filaments from fragmentation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Article
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Microtubule damage shapes the acetylation gradient.Nature communications · 2024Article
- Microtubule acetylation dyshomeostasis in Parkinson's disease.Translational neurodegeneration · 2023Review
- Causes, costs and consequences of kinesin motors communicating through the microtubule lattice.Journal of cell science · 2023Article
- The effect of motor-induced shaft dynamics on microtubule stability and length.Biophysical journal · 2023Article
- The rate of microtubule breaking increases exponentially with curvature.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Severing enzymes and molecular motors extract tubulin from the walls of microtubules by exerting mechanical force on subunits buried in the lattice. However, how much force is needed to remove tubulin from microtubules is not known, nor is the pathway by which subunits are removed. Using a site-specific functionalization method, we applied forces to the C-terminus of α-tubulin with an optical tweezer and found that a force of ~30 pN is required to extract tubulin from the microtubule wall. Additionally, we discovered that partial unfolding is an intermediate step in tubulin removal. The unfolding and extraction forces are similar to those generated by AAA-unfoldases. Lastly, we show that three kinesin-1 motor proteins can also extract tubulin from the microtubule lattice. Our results provide the first experimental investigation of how tubulin responds to mechanical forces exerted on its α-tubulin C-terminal tail and have implications for the mechanisms of severing enzymes and microtubule stability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.