ArticleNature2008
Direct observation of the mechanochemical coupling in myosin Va during processive movement.
Article in Nature, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
67 citing papers in PubMed, 136 citations in OpenAlex.
- Coupling between the lever arm and active site via an N-terminal extension tunes force sensitivity in the myosin-1 family.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Expression, Purification, and In Vitro Analysis of Myosin.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Myosin-5 varies its step length to carry cargo straight along the irregular F-actin track.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Switch-2 determines MgFrontiers in physiology · 2024Article
- Myosin-5 varies its steps along the irregular F-actin track.bioRxiv : the preprint server for biology · 2023Article
- Direct identification of the rotary angle of ATP cleavage in FBiophysical journal · 2023Article
- Information flow, gating, and energetics in dimeric molecular motors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Modulating mechanical stability of heterodimerization between engineered orthogonal helical domains.Nature communications · 2020Article
- Studies on the impellers generating force in muscle.Biophysical reviews · 2020Article
- Article
- A Generalized Kinetic Model for Coupling between Stepping and ATP Hydrolysis of Kinesin Molecular Motors.International journal of molecular sciences · 2019Article
- A model for the chemomechanical coupling of the mammalian cytoplasmic dynein molecular motor.European biophysics journal : EBJ · 2019Article
- A model for the chemomechanical coupling of myosin-V molecular motors.RSC advances · 2019Article
- A Unified Walking Model for Dimeric Motor Proteins.Biophysical journal · 2018Article
- Designed Elastic Networks: Models of Complex Protein Machinery.International journal of molecular sciences · 2018Review
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
- Direct AFM Visualization of the Nanoscale Dynamics of Biomolecular Complexes.Journal of physics D: Applied physics · 2018Article
- Kinetic signatures of myosin-5B, the motor involved in microvillus inclusion disease.The Journal of biological chemistry · 2017Article
- Reexamining the origin of the directionality of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
7 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
5 authors at 2 institutions in 1 country.
Funding
Abstract
Myosin Va transports intracellular cargoes along actin filaments in cells. This processive, two-headed motor takes multiple 36-nm steps in which the two heads swing forward alternately towards the barbed end of actin driven by ATP hydrolysis. The ability of myosin Va to move processively is a function of its long lever arm, the high duty ratio of its kinetic cycle and the gating of the kinetics between the two heads such that ADP release from the lead head is greatly retarded. Mechanical studies at the multiple- and the single-molecule level suggest that there is tight coupling (that is, one ATP is hydrolysed per power stroke), but this has not been directly demonstrated. We therefore investigated the coordination between the ATPase mechanism of the two heads of myosin Va and directly visualized the binding and dissociation of single fluorescently labelled nucleotide molecules, while simultaneously observing the stepping motion of the fluorescently labelled myosin Va as it moved along an actin filament. Here we show that preferential ADP dissociation from the trail head of mouse myosin Va is followed by ATP binding and a synchronous 36-nm step. Even at low ATP concentrations, the myosin Va molecule retained at least one nucleotide (ADP in the lead head position) when moving. Thus, we directly demonstrate tight coupling between myosin Va movement and the binding and dissociation of nucleotide by simultaneously imaging with near nanometre precision.
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What OpenQuestion holds
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.