ArticleNature chemical biology2017
Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- In vitro reconstitution defines the mechanistic basis of HSET motor activity regulation by IntraFlagellar Transport proteins.Communications biology · 2026Article
- The tail domain of the plant kinesin-12 POK2 is a versatile interaction hub.Journal of cell science · 2025Article
- 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
- Molecular design principles for bipolar spindle organization by two opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Insights into the role of phosphorylation on microtubule cross-linking by PRC1.Molecular biology of the cell · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Force-transducing molecular ensembles at growing microtubule tips control mitotic spindle size.Nature communications · 2024Article
- Microtubule choreography: spindle self-organization during cell division.Biophysical reviews · 2024Review
- Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes.Nature communications · 2024Article
- Modeling Studies of the Mechanism of Context-Dependent Bidirectional Movements of Kinesin-14 Motors.Molecules (Basel, Switzerland) · 2024Article
- Phosphorylation controls spatial and temporal activities of motor-PRC1 complexes to complete mitosis.The EMBO journal · 2023Article
- Electro-detachment of kinesin motor domain from microtubule in silico.Computational and structural biotechnology journal · 2023Article
- Cross-linker design determines microtubule network organization by opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- KIFC1 Regulates the Trajectory of Neuronal Migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- TheInternational journal of molecular sciences · 2021Article
- Anillin propels myosin-independent constriction of actin rings.Nature communications · 2021Article
- Micron-scale geometrical features of microtubules as regulators of microtubule organization.eLife · 2021Review
- Klp2 and Ase1 synergize to maintain meiotic spindle stability during metaphase I.The Journal of biological chemistry · 2020Article
- IFT proteins interact with HSET to promote supernumerary centrosome clustering in mitosis.EMBO reports · 2020Article
- Kinesin-14 motors drive a right-handed helical motion of antiparallel microtubules around each other.Nature communications · 2020Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubule-crosslinking motor proteins, which slide antiparallel microtubules, are required for the remodeling of microtubule networks. Hitherto, all microtubule-crosslinking motors have been shown to slide microtubules at a constant velocity until no overlap remains between them, leading to the breakdown of the initial microtubule geometry. Here, we show in vitro that the sliding velocity of microtubules, driven by human kinesin-14 HSET, decreases when microtubules start to slide apart, resulting in the maintenance of finite-length microtubule overlaps. We quantitatively explain this feedback using the local interaction kinetics of HSET with overlapping microtubules that cause retention of HSET in shortening overlaps. Consequently, the increased HSET density in the overlaps leads to a density-dependent decrease in sliding velocity and the generation of an entropic force that antagonizes the force exerted by the motors. Our results demonstrate that a spatial arrangement of microtubules can regulate the collective action of molecular motors through the local alteration of their individual interaction kinetics.
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