ArticleeLife2015
Examining kinesin processivity within a general gating framework.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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Who cites it
93 citing papers in PubMed.
- Article
- 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
- Mitochondrial position responds to glucose stimulation in a model of the pancreatic beta cell.Biophysical journal · 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
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.Molecular biology of the cell · 2025Article
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping.The Journal of cell biology · 2025Article
- PRC1 resists microtubule sliding in two distinct resistive modes due to variations in the separation between overlapping microtubules.bioRxiv : the preprint server for biology · 2025Article
- Kinetic regulation of kinesin's two motor domains coordinates its stepping along microtubules.eLife · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Tether-scanning the kinesin motor domain reveals a core mechanical action.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Competition between physical search and a weak-to-strong transition rate-limits kinesin binding times.PLoS computational biology · 2024Article
- A Model for Chemomechanical Coupling of Kinesin-3 Motor.Cellular and molecular bioengineering · 2024Article
- Article
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- New insights into the mechanochemical coupling mechanism of kinesin-microtubule complexes from their high-resolution structures.Biochemical Society transactions · 2023Review
- Simulations suggest robust microtubule attachment of kinesin and dynein in antagonistic pairs.Biophysical journal · 2023Article
33 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors.
Funding
Abstract
Kinesin-1 is a dimeric motor that transports cargo along microtubules, taking 8.2-nm steps in a hand-over-hand fashion. The ATP hydrolysis cycles of its two heads are maintained out of phase by a series of gating mechanisms, which lead to processive runs averaging ~1 μm. A key structural element for inter-head coordination is the neck linker (NL), which connects the heads to the stalk. To examine the role of the NL in regulating stepping, we investigated NL mutants of various lengths using single-molecule optical trapping and bulk fluorescence approaches in the context of a general framework for gating. Our results show that, although inter-head tension enhances motor velocity, it is crucial neither for inter-head coordination nor for rapid rear-head release. Furthermore, cysteine-light mutants do not produce wild-type motility under load. We conclude that kinesin-1 is primarily front-head gated, and that NL length is tuned to enhance unidirectional processivity and velocity.
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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.