ArticleBiophysical journal2013
The kinetics of mechanically coupled myosins exhibit group size-dependent regimes.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk Using QCM-D.Cellular and molecular bioengineering · 2025Article
- Measuring emergent mechanical changes in cytoskeletal ensemblesFrontiers in cell and developmental biology · 2025Article
- Deciphering Mechanochemical Influences of Emergent Actomyosin Crosstalk using QCM-D.bioRxiv : the preprint server for biology · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- Cooperativity of myosin II motors in the non-regulated and regulated thin filaments investigated with high-speed AFM.The Journal of general physiology · 2023Article
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
- Force-velocity and tension transient measurements from Drosophila jump muscle reveal the necessity of both weakly-bound cross-bridges and series elasticity in models of muscle contraction.Archives of biochemistry and biophysics · 2021Article
- Spreading of perturbations in myosin group kinetics along actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Rapid time-stamped analysis of filament motility.Journal of muscle research and cell motility · 2018Article
- Chemomechanical regulation of myosin Ic cross-bridges: Deducing the elastic properties of an ensemble from single-molecule mechanisms.PLoS computational biology · 2017Article
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Engineering Circular Gliding of Actin Filaments Along Myosin-Patterned DNA Nanotube Rings To Study Long-Term Actin-Myosin Behaviors.ACS nano · 2016Article
- Simultaneous nano-tracking of multiple motor proteins via spectral discrimination of quantum dots.Biomedical optics express · 2016Article
- Mechanical coordination in motor ensembles revealed using engineered artificial myosin filaments.Nature nanotechnology · 2015Article
- Isoforms Confer Characteristic Force Generation and Mechanosensation by Myosin II Filaments.Biophysical journal · 2015Article
- Phosphate and ADP differently inhibit coordinated smooth muscle myosin groups.Biophysical journal · 2015Article
- The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2014Article
- Molecular mechanical differences between isoforms of contractile actin in the presence of isoforms of smooth muscle tropomyosin.PLoS computational biology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Naturally occurring groups of muscle myosin behave differently from individual myosins or small groups commonly assayed in vitro. Here, we investigate the emergence of myosin group behavior with increasing myosin group size. Assuming the number of myosin binding sites (N) is proportional to actin length (L) (N = L/35.5 nm), we resolve in vitro motility of actin propelled by skeletal muscle myosin for L = 0.2-3 μm. Three distinct regimes were found: L < 0.3 μm, sliding arrest; 0.3 μm ≤ L ≤ 1 μm, alternation between arrest and continuous sliding; L > 1 μm, continuous sliding. We theoretically investigated the myosin group kinetics with mechanical coupling via actin. We find rapid actin sliding steps driven by power-stroke cascades supported by postpower-stroke myosins, and phases without actin sliding caused by prepower-stroke myosin buildup. The three regimes are explained: N = 8, rare cascades; N = 15, cascade bursts; N = 35, continuous cascading. Two saddle-node bifurcations occur for increasing N (mono → bi → mono-stability), with steady states corresponding to arrest and continuous cascading. The experimentally measured dependence of actin sliding statistics on L and myosin concentration is correctly predicted.
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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.