ArticleProceedings of the National Academy of Sciences of the United States of America2015
Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
70 citing papers in PubMed, 142 citations in OpenAlex.
- Neck region-microtubule interactions direct counterclockwise stepping of kinesin-1.Biophysical journal · 2026Article
- Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.Biophysical journal · 2026Article
- Article
- Oxidative stress impairs processive motility of the axonal transport motor KIF1A.The Journal of biological chemistry · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak interhead coordination.Biophysical journal · 2026Article
- ATPγS substantially defeats the biasing mechanism for kinesin steps.Nature communications · 2026Article
- Dimeric Cin8 motors have an inherent plus-end bias and weak inter-head coordination.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
- DNA tensiometer reveals catch-bond detachment kinetics of kinesin-1, -2 and -3.bioRxiv : the preprint server for biology · 2025Article
- Factors Determining Kinesin Motors in a Predominant One-Head-Bound or Two-Heads-Bound State During Its Stepping Cycle.Biomolecules · 2025Article
- MINFLUX achieves molecular resolution with minimal photons.Nature photonics · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Tracking Single Kinesin in Live Cells Using MINFLUX.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Dissecting the pH Sensitivity of Kinesin-Driven Transport.The journal of physical chemistry. B · 2024Article
- Nonthermal fluctuations accelerate biomolecular motors.Biophysical reviews · 2024Review
- Uncovering kinesin dynamics in neurites with MINFLUX.Communications biology · 2024Article
- Modeling the motion of disease-associated KIF1A heterodimers.Biophysical journal · 2023Article
- Article
- 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
- CLASP2 recognizes tubulins exposed at the microtubule plus-end in a nucleotide state-sensitive manner.Science advances · 2023Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
To dissect the kinetics of structural transitions underlying the stepping cycle of kinesin-1 at physiological ATP, we used interferometric scattering microscopy to track the position of gold nanoparticles attached to individual motor domains in processively stepping dimers. Labeled heads resided stably at positions 16.4 nm apart, corresponding to a microtubule-bound state, and at a previously unseen intermediate position, corresponding to a tethered state. The chemical transitions underlying these structural transitions were identified by varying nucleotide conditions and carrying out parallel stopped-flow kinetics assays. At saturating ATP, kinesin-1 spends half of each stepping cycle with one head bound, specifying a structural state for each of two rate-limiting transitions. Analysis of stepping kinetics in varying nucleotides shows that ATP binding is required to properly enter the one-head-bound state, and hydrolysis is necessary to exit it at a physiological rate. These transitions differ from the standard model in which ATP binding drives full docking of the flexible neck linker domain of the motor. Thus, this work defines a consensus sequence of mechanochemical transitions that can be used to understand functional diversity across the kinesin superfamily.
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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.