ArticleDevelopmental cell2015
Measuring Pushing and Braking Forces Generated by Ensembles of Kinesin-5 Crosslinking Two Microtubules.
Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed.
- Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.Biophysical journal · 2026Article
- Molecular Dynamics Simulations Provide Further Insights into the Allosteric Regulation of the Kinesin-5 Motor Domain by Loop 5.Journal of chemical information and modeling · 2026Article
- Midzone bundles of the mammalian anaphase spindle are mechanically coupled both locally and globally.bioRxiv : the preprint server for biology · 2026Article
- Stall force measurement of the kinesin-3 motor KIF1A using a programmable DNA origami nanospring.eLife · 2026Article
- Factors Determining Kinesin Motors in a Predominant One-Head-Bound or Two-Heads-Bound State During Its Stepping Cycle.Biomolecules · 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
- Kinesin-5/Cut7 C-terminal tail phosphorylation is essential for microtubule sliding force and bipolar mitotic spindle assembly.Current biology : CB · 2024Article
- Force generation and resistance in human mitosis.Biophysical reviews · 2024Review
- Cell motility, cytoskeleton, and motor proteins-21st IUPAB Congress session commentary.Biophysical reviews · 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
- Antiparallel microtubule bundling supports KIF15-driven mitotic spindle assembly.Molecular biology of the cell · 2024Article
- A stable microtubule bundle formed through an orchestrated multistep process controls quiescence exit.eLife · 2024Article
- Mitotic Functions and Characters of KIF11 in Cancers.Biomolecules · 2024Review
- Article
- Fundamentals of Mechanobiology and Potential Applications in Spinal Fusion.International journal of spine surgery · 2023Article
- Redundant microtubule crosslinkers prevent meiotic spindle bending to ensure diploid offspring in C. elegans.PLoS genetics · 2023Article
- The kinesin-5 tail and bipolar minifilament domains are the origin of its microtubule crosslinking and sliding activity.Molecular biology of the cell · 2023Article
- Distinct regions of the kinesin-5 C-terminal tail are essential for mitotic spindle midzone localization and sliding force.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
28 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
The proper organization of the microtubule-based mitotic spindle is proposed to depend on nanometer-sized motor proteins generating forces that scale with a micron-sized geometric feature, such as microtubule overlap length. However, it is unclear whether such regulation can be achieved by any mitotic motor protein. Here, we employ an optical-trap- and total internal reflection fluorescence (TIRF)-based assay to show that ensembles of kinesin-5, a conserved mitotic motor protein, can push apart overlapping antiparallel microtubules to generate a force whose magnitude scales with filament overlap length. We also find that kinesin-5 can produce overlap-length-dependent "brake-like" resistance against relative microtubule sliding in both parallel and antiparallel geometries, an activity that has been suggested by cell biological studies but had not been directly measured. Together, these findings, along with numerical simulations, reveal how a motor protein can function as an analog converter, "reading" simple geometric and dynamic features in cytoskeletal networks to produce regulated force outputs.
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