ArticleProceedings of the National Academy of Sciences of the United States of America2016
Schizosaccharomyces pombe kinesin-5 switches direction using a steric blocking mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.Biophysical journal · 2026Article
- Feedback between filament spacing, crosslinker binding, and self-organization in cytoskeletal bundles.bioRxiv : the preprint server for biology · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.bioRxiv : the preprint server for biology · 2025Article
- PP6 phosphatase and Elongator contribute to kinesin 5-dependent spindle assembly by controlling microtubule regulators levels.PLoS genetics · 2025Article
- Measuring molecular forces inside living cells using magnetic tweezers.Biophysical reviews · 2025Review
- Selective regulation of kinesin-5 function by β-tubulin carboxy-terminal tails.The Journal of cell biology · 2025Article
- Kinesin-5/Cut7 C-terminal tail phosphorylation is essential for microtubule sliding force and bipolar mitotic spindle assembly.Current biology : CB · 2024Article
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- 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
- The kinesin-5 protein Cut7 moves bidirectionally on fission yeast spindles with activity that increases in anaphase.Journal of cell science · 2023Article
- Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules.Scientific reports · 2022Article
- The microtubule plus-end tracking protein Bik1 is required for chromosome congression.Molecular biology of the cell · 2022Article
- Kinesin Motors in the Filamentous Basidiomycetes in Light of theJournal of fungi (Basel, Switzerland) · 2022Review
- Using a comprehensive approach to investigate the interaction between Kinesin-5/Eg5 and the microtubule.Computational and structural biotechnology journal · 2022Article
- Modeling spatiotemporally varying protein-protein interactions in CyLaKS, the Cytoskeleton Lattice-based Kinetic Simulator.The European physical journal. E, Soft matter · 2021Article
- Article
- Flexible microtubule anchoring modulates the bi-directional motility of the kinesin-5 Cin8.Cellular and molecular life sciences : CMLS · 2021Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Drag-induced directionality switching of kinesin-5 Cin8 revealed by cluster-motility analysis.Science advances · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Cut7, the sole kinesin-5 in Schizosaccharomyces pombe, is essential for mitosis. Like other yeast kinesin-5 motors, Cut7 can reverse its stepping direction, by mechanisms that are currently unclear. Here we show that for full-length Cut7, the key determinant of stepping direction is the degree of motor crowding on the microtubule lattice, with greater crowding converting the motor from minus end-directed to plus end-directed stepping. To explain how high Cut7 occupancy causes this reversal, we postulate a simple proximity sensing mechanism that operates via steric blocking. We propose that the minus end-directed stepping action of Cut7 is selectively inhibited by collisions with neighbors under crowded conditions, whereas its plus end-directed action, being less space-hungry, is not. In support of this idea, we show that the direction of Cut7-driven microtubule sliding can be reversed by crowding it with non-Cut7 proteins. Thus, crowding by either dynein microtubule binding domain or Klp2, a kinesin-14, converts Cut7 from net minus end-directed to net plus end-directed stepping. Biochemical assays confirm that the Cut7 N terminus increases Cut7 occupancy by binding directly to microtubules. Direct observation by cryoEM reveals that this occupancy-enhancing N-terminal domain is partially ordered. Overall, our data point to a steric blocking mechanism for directional reversal through which collisions of Cut7 motor domains with their neighbors inhibit their minus end-directed stepping action, but not their plus end-directed stepping action. Our model can potentially reconcile a number of previous, apparently conflicting, observations and proposals for the reversal mechanism of yeast kinesins-5.
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