ArticleeLife2020
The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Kinesin-5/Cut7 C-terminal tail phosphorylation influence on motor regulation through multi-scale molecular modeling.Biophysical journal · 2026Article
- Capillary bundling of microtubules by condensates.bioRxiv : the preprint server for biology · 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
- Intellectual disability-causing mutations in KIF11 impair microtubule dynamics and dendritic arborization.Nature communications · 2026Article
- 'Mitotic' kinesin-5 is a dynamic brake for axonal growth in Drosophila.Development (Cambridge, England) · 2025Article
- Selective regulation of kinesin-5 function by β-tubulin carboxy-terminal tails.The Journal of cell biology · 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
- Microtubule choreography: spindle self-organization during cell division.Biophysical reviews · 2024Review
- Human kinesin-5 KIF11 drives the helical motion of anti-parallel and parallel microtubules around each other.The EMBO journal · 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
- Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin.Science advances · 2024Article
- 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
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- Cortical dynein drives centrosome clustering in cells with centrosome amplification.Molecular biology of the cell · 2023Article
- The kinesin-5 protein Cut7 moves bidirectionally on fission yeast spindles with activity that increases in anaphase.Journal of cell science · 2023Article
- Effects of microtubule length and crowding on active microtubule network organization.iScience · 2023Article
- Multi-curve fitting and tubulin-lattice signal removal for structure determination of large microtubule-based motors.Journal of structural biology · 2022Article
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
Kinesin-5 motors organize mitotic spindles by sliding apart microtubules. They are homotetramers with dimeric motor and tail domains at both ends of a bipolar minifilament. Here, we describe a regulatory mechanism involving direct binding between tail and motor domains and its fundamental role in microtubule sliding. Kinesin-5 tails decrease microtubule-stimulated ATP-hydrolysis by specifically engaging motor domains in the nucleotide-free or ADP states. Cryo-EM reveals that tail binding stabilizes an open motor domain ATP-active site. Full-length motors undergo slow motility and cluster together along microtubules, while tail-deleted motors exhibit rapid motility without clustering. The tail is critical for motors to zipper together two microtubules by generating substantial sliding forces. The tail is essential for mitotic spindle localization, which becomes severely reduced in tail-deleted motors. Our studies suggest a revised microtubule-sliding model, in which kinesin-5 tails stabilize motor domains in the microtubule-bound state by slowing ATP-binding, resulting in high-force production at both homotetramer ends.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.