ArticleBiophysical journal2013
Kinesin-8 is a low-force motor protein with a weakly bound slip state.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Article
- Mechanical states of a motor protein in the spindle.Current biology : CB · 2026Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Determinant factors for residence time of kinesin motors at microtubule ends.Journal of biological physics · 2023Article
- KIF1A is kinetically tuned to be a superengaging motor under hindering loads.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Directly Measuring Forces within Reconstituted Active Microtubule Bundles.Journal of visualized experiments : JoVE · 2022Article
- Calculating the force-dependent unbinding rate of biological macromolecular bonds from force-ramp optical trapping assays.Scientific reports · 2022Article
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
- A model of processive walking and slipping of kinesin-8 molecular motors.Scientific reports · 2021Article
- Backstepping Mechanism of Kinesin-1.Biophysical journal · 2020Article
- Polycationic gold nanorods as multipurposeNanoscale advances · 2020Article
- These motors were made for walking.Protein science : a publication of the Protein Society · 2020Review
- Review
- The Kinesin-8 Kip3 Depolymerizes Microtubules with a Collective Force-Dependent Mechanism.Biophysical journal · 2020Article
- Tubulin tails and their modifications regulate protein diffusion on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Three-Dimensional Optical Tweezers Tracking Resolves Random Sideward Steps of the Kinesin-8 Kip3.Biophysical journal · 2018Article
- Directionally biased sidestepping of Kip3/kinesin-8 is regulated by ATP waiting time and motor-microtubule interaction strength.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Phragmoplast Orienting Kinesin 2 Is a Weak Motor Switching between Processive and Diffusive Modes.Biophysical journal · 2018Article
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5 authors.
Funding
Abstract
During the cell cycle, kinesin-8s control the length of microtubules by interacting with their plus ends. To reach these ends, the motors have to be able to take many steps without dissociating. However, the underlying mechanism for this high processivity and how stepping is affected by force are unclear. Here, we tracked the motion of yeast (Kip3) and human (Kif18A) kinesin-8s with high precision under varying loads using optical tweezers. Surprisingly, both kinesin-8 motors were much weaker compared with other kinesins. Furthermore, we discovered a force-induced stick-slip motion: the motor frequently slipped, recovered from this state, and then resumed normal stepping motility without detaching from the microtubule. The low forces are consistent with kinesin-8s being regulators of microtubule dynamics rather than cargo transporters. The weakly bound slip state, reminiscent of a molecular safety leash, may be an adaptation for high processivity.
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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.