ArticleProceedings of the National Academy of Sciences of the United States of America2014
Kinesin processivity is gated by phosphate release.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- Characterizing dynamics of productive dynein stepping by MINFLUX.Nature structural & molecular biology · 2026Article
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- Enhanced processivity and collective force production of kinesin-1 at low radial forces.eLife · 2026Article
- Feedback between filament spacing, crosslinker binding, and self-organization in cytoskeletal bundles.bioRxiv : the preprint server for biology · 2026Article
- Enhanced Processivity and Collective Force Production of Kinesin-1 at Low Radial Forces.bioRxiv : the preprint server for biology · 2025Article
- An Overview of Contrasting Experimental Results on Dynamics of Kinesin-1 Molecular Motors: Insight into the Underlying Mechanism.Biomolecules · 2025Review
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- Nonthermal fluctuations accelerate biomolecular motors.Biophysical reviews · 2024Review
- Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.Nature communications · 2024Article
- Competition between physical search and a weak-to-strong transition rate-limits kinesin binding times.PLoS computational biology · 2024Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- ADP release can explain spatially-dependent kinesin binding times.bioRxiv : the preprint server for biology · 2023Article
- On the use of thermal forces to probe kinesin's response to force.Frontiers in molecular biosciences · 2023Article
- Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation.Nature communications · 2022Article
- Microtubule Dumbbells to Assess the Effect of Force Geometry on Single Kinesin Motors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Tuning ensemble-averaged cargo run length via fractional change in mean kinesin number.Physical biology · 2021Article
- Review
- A kinetic dissection of the fast and superprocessive kinesin-3 KIF1A reveals a predominant one-head-bound state during its chemomechanical cycle.The Journal of biological chemistry · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
Abstract
Kinesin-1 is a dimeric motor protein, central to intracellular transport, that steps hand-over-hand toward the microtubule (MT) plus-end, hydrolyzing one ATP molecule per step. Its remarkable processivity is critical for ferrying cargo within the cell: over 100 successive steps are taken, on average, before dissociation from the MT. Despite considerable work, it is not understood which features coordinate, or "gate," the mechanochemical cycles of the two motor heads. Here, we show that kinesin dissociation occurs subsequent to, or concomitant with, phosphate (P(i)) release following ATP hydrolysis. In optical trapping experiments, we found that increasing the steady-state population of the posthydrolysis ADP · P(i) state (by adding free P(i)) nearly doubled the kinesin run length, whereas reducing either the ATP binding rate or hydrolysis rate had no effect. The data suggest that, during processive movement, tethered-head binding occurs subsequent to hydrolysis, rather than immediately after ATP binding, as commonly suggested. The structural change driving motility, thought to be neck linker docking, is therefore completed only upon hydrolysis, and not ATP binding. Our results offer additional insights into gating mechanisms and suggest revisions to prevailing models of the kinesin reaction cycle.
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