ArticleProceedings of the National Academy of Sciences of the United States of America2013
Measuring collective transport by defined numbers of processive and nonprocessive kinesin motors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 113 papers.
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Who cites it
113 citing papers in PubMed.
- Enhanced processivity and collective force production of kinesin-1 at low radial forces.eLife · 2026Article
- In vitro reconstitution defines the mechanistic basis of HSET motor activity regulation by IntraFlagellar Transport proteins.Communications biology · 2026Article
- Stall force measurement of the kinesin-3 motor KIF1A using a programmable DNA origami nanospring.eLife · 2026Article
- Molecular Motors Orchestrate Pause-and-Run Dynamics to Facilitate Intracellular Transport.Biomolecules · 2026Article
- Mechanical states of a motor protein in the spindle.Current biology : CB · 2026Article
- Active fluctuations of cytoplasmic actomyosin networks facilitate dynein-driven transport.iScience · 2025Article
- Enhanced Processivity and Collective Force Production of Kinesin-1 at Low Radial Forces.bioRxiv : the preprint server for biology · 2025Article
- Kinesin-1 autoinhibition tunes cargo transport by motor ensembles.Biophysical journal · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.Molecular biology of the cell · 2025Article
- Protocol for assembling photostable fluorescence-labeled tiny DNA origami blocks to observe kinesin cooperation.STAR protocols · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.bioRxiv : the preprint server for biology · 2025Article
- Motor-driven microtubule diffusion in a photobleached dynamical coordinate system.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Motor clustering enhances kinesin-driven vesicle transport.Biophysical journal · 2025Article
- Nuclear deformation by microtubule molecular motors.PLoS computational biology · 2025Article
- Impact of physiological ionic strength and crowding on kinesin-1 motility.Cell structure and function · 2025Article
- Multiple kinesins speed up cargo transport in crowded environments by sharing load.Communications biology · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- 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
- Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intracellular transport is thought to be achieved by teams of motor proteins bound to a cargo. However, the coordination within a team remains poorly understood as a result of the experimental difficulty in controlling the number and composition of motors. Here, we developed an experimental system that links together defined numbers of motors with defined spacing on a DNA scaffold. By using this system, we linked multiple molecules of two different types of kinesin motors, processive kinesin-1 or nonprocessive Ncd (kinesin-14), in vitro. Both types of kinesins markedly increased their processivities with motor number. Remarkably, despite the poor processivity of individual Ncd motors, the coupling of two Ncd motors enables processive movement for more than 1 μm along microtubules (MTs). This improvement was further enhanced with decreasing spacing between motors. Force measurements revealed that the force generated by groups of Ncd is additive when two to four Ncd motors work together, which is much larger than that generated by single motors. By contrast, the force of multiple kinesin-1s depends only weakly on motor number. Numerical simulations and single-molecule unbinding measurements suggest that this additive nature of the force exerted by Ncd relies on fast MT binding kinetics and the large drag force of individual Ncd motors. These features would enable small groups of Ncd motors to crosslink MTs while rapidly modulating their force by forming clusters. Thus, our experimental system may provide a platform to study the collective behavior of motor proteins from the bottom up.
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