ArticleNature communications2018
Diffusive tail anchorage determines velocity and force produced by kinesin-14 between crosslinked microtubules.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.Molecular biology of the cell · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Tubulin sequence divergence is associated with the use of distinct microtubule regulators.Current biology : CB · 2025Article
- Force-transducing molecular ensembles at growing microtubule tips control mitotic spindle size.Nature communications · 2024Article
- An internally controlled system to study microtubule network diversification links tubulin evolution to the use of distinct microtubule regulators.bioRxiv : the preprint server for biology · 2024Article
- Optical tweezers across scales in cell biology.Trends in cell biology · 2022Review
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
- Cross-linker design determines microtubule network organization by opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Diffusion of kinesin motors on cargo can enhance binding and run lengths during intracellular transport.Molecular biology of the cell · 2021Article
- Klp2 and Ase1 synergize to maintain meiotic spindle stability during metaphase I.The Journal of biological chemistry · 2020Article
- Kinesin-14 motors drive a right-handed helical motion of antiparallel microtubules around each other.Nature communications · 2020Article
- Different motilities of microtubules driven by kinesin-1 and kinesin-14 motors patterned on nanopillars.Science advances · 2020Article
- Bidirectional sliding of two parallel microtubules generated by multiple identical motors.Journal of mathematical biology · 2019Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Form and function of the mitotic spindle depend on motor proteins that crosslink microtubules and move them relative to each other. Among these are kinesin-14s, such as Ncd, which interact with one microtubule via their non-processive motor domains and with another via their diffusive tail domains, the latter allowing the protein to slip along the microtubule surface. Little is known about the influence of the tail domains on the protein's performance. Here, we show that diffusive anchorage of Ncd's tail domains impacts velocity and force considerably. Tail domain slippage reduced velocities from 270 nm s
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