ArticleThe Journal of biological chemistry2015
Deletion of the Tail Domain of the Kinesin-5 Cin8 Affects Its Directionality.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Nano fountain pen patterning of microtubule tracks for guiding molecular motors.Scientific reports · 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
- 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
- The kinesin-5 protein Cut7 moves bidirectionally on fission yeast spindles with activity that increases in anaphase.Journal of cell science · 2023Article
- Using a comprehensive approach to investigate the interaction between Kinesin-5/Eg5 and the microtubule.Computational and structural biotechnology journal · 2022Article
- 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
- Article
- Synthetic-Evolution Reveals Narrow Paths to Regulation of theInternational journal of biological sciences · 2019Article
- Bidirectional motility of kinesin-5 motor proteins: structural determinants, cumulative functions and physiological roles.Cellular and molecular life sciences : CMLS · 2018Review
- Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding.Nature chemical biology · 2017Article
- Ensembles of Bidirectional Kinesin Cin8 Produce Additive Forces in Both Directions of Movement.Biophysical journal · 2017Article
- Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase.Cellular and molecular life sciences : CMLS · 2017Article
- The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.The Journal of biological chemistry · 2017Article
- Embedding dual function into molecular motors through collective motion.Scientific reports · 2017Article
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10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bipolar kinesin-5 motors are one of the major players that govern mitotic spindle dynamics. Their bipolar structure enables them to cross-link and slide apart antiparallel microtubules (MTs) emanating from the opposing spindle poles. The budding yeast kinesin-5 Cin8 was shown to switch from fast minus-end- to slow plus-end-directed motility upon binding between antiparallel MTs. This unexpected finding revealed a new dimension of cellular control of transport, the mechanism of which is unknown. Here we have examined the role of the C-terminal tail domain of Cin8 in regulating directionality. We first constructed a stable dimeric Cin8/kinesin-1 chimera (Cin8Kin), consisting of head and neck linker of Cin8 fused to the stalk of kinesin-1. As a single dimeric motor, Cin8Kin switched frequently between plus and minus directionality along single MTs, demonstrating that the Cin8 head domains are inherently bidirectional, but control over directionality was lost. We next examined the activity of a tetrameric Cin8 lacking only the tail domains (Cin8Δtail). In contrast to wild-type Cin8, the motility of single molecules of Cin8Δtail in high ionic strength was slow and bidirectional, with almost no directionality switches. Cin8Δtail showed only a weak ability to cross-link MTs in vitro. In vivo, Cin8Δtail exhibited bias toward the plus-end of the MTs and was unable to support viability of cells as the sole kinesin-5 motor. We conclude that the tail of Cin8 is not necessary for bidirectional processive motion, but is controlling the switch between plus- and minus-end-directed motility.
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