ArticleThe Journal of biological chemistry2012
Collective dynamics of elastically coupled myosin V motors.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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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.
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Who cites it
27 citing papers in PubMed, 55 citations in OpenAlex.
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.eLife · 2024Article
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.bioRxiv : the preprint server for biology · 2024Article
- Cargo properties play a critical role in myosin Va-driven cargo transport along actin filaments.Biochemistry and biophysics reports · 2022Article
- Cargo adaptors regulate stepping and force generation of mammalian dynein-dynactin.Nature chemical biology · 2019Article
- Force sharing and force generation by two teams of elastically coupled molecular motors.Scientific reports · 2019Article
- Dissecting myosin-5B mechanosensitivity and calcium regulation at the single molecule level.Nature communications · 2018Article
- Molecular origin of the weak susceptibility of kinesin velocity to loads and its relation to the collective behavior of kinesins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Small teams of myosin Vc motors coordinate their stepping for efficient cargo transport on actin bundles.The Journal of biological chemistry · 2017Article
- Cargo Transport by Two Coupled Myosin Va Motors on Actin Filaments and Bundles.Biophysical journal · 2016Article
- Transport efficiency of membrane-anchored kinesin-1 motors depends on motor density and diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- Simultaneous nano-tracking of multiple motor proteins via spectral discrimination of quantum dots.Biomedical optics express · 2016Article
- Collective dynamics of processive cytoskeletal motors.Soft matter · 2016Review
- Biological machines: Molecular motor teamwork.Nature nanotechnology · 2015Article
- Mechanical coordination in motor ensembles revealed using engineered artificial myosin filaments.Nature nanotechnology · 2015Article
- Article
- A method for multiprotein assembly in cells reveals independent action of kinesins in complex.The Journal of cell biology · 2014Article
- Motor coupling through lipid membranes enhances transport velocities for ensembles of myosin Va.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Myosin lever arm directs collective motion on cellular actin network.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Delineating cooperative responses of processive motors in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Characterization of the collective behaviors of different classes of processive motor proteins has become increasingly important to understand various intracellular trafficking and transport processes. This work examines the dynamics of structurally-defined motor complexes containing two myosin Va (myoVa) motors that are linked together via a molecular scaffold formed from a single duplex of DNA. Dynamic changes in the filament-bound configuration of these complexes due to motor binding, stepping, and detachment were monitored by tracking the positions of different color quantum dots that report the position of one head of each myoVa motor on actin. As in studies of multiple kinesins, the run lengths produced by two myosins are only slightly larger than those of single motor molecules. This suggests that internal strain within the complexes, due to asynchronous motor stepping and the resultant stretching of motor linkages, yields net negative cooperative behaviors. In contrast to multiple kinesins, multiple myosin complexes move with appreciably lower velocities than a single-myosin molecule. Although similar trends are predicted by a discrete state stochastic model of collective motor dynamics, these analyses also suggest that multiple myosin velocities and run lengths depend on both the compliance and the effective size of their cargo. Moreover, it is proposed that this unique collective behavior occurs because the large step size and relatively small stalling force of myoVa leads to a high sensitivity of motor stepping rates to strain.
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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.