ArticleProceedings of the National Academy of Sciences of the United States of America2021
Evolution of mechanical cooperativity among myosin II motors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- An Expanded Markov State Model-Transition Path Theory Framework for Ion Conduction Reactive Pathways through Membrane Channels.The journal of physical chemistry letters · 2026Article
- Light-induced assembly and repeatable actuation in CaNature communications · 2026Article
- Multistate Kinetic Model of the Sodium-Potassium ATPase.The journal of physical chemistry. B · 2025Article
- The advancement of biosensor design and construction utilizing biomolecular motors.Synthetic and systems biotechnology · 2025Review
- How Omecamtiv Modulates Myosin Motion.Biochemistry · 2025Article
- 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
- Myosin II Adjusts Motility Properties and Regulates Force Production Based on Motor Environment.Cellular and molecular bioengineering · 2022Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin II is a biomolecular machine that is responsible for muscle contraction. Myosin II motors act cooperatively: during muscle contraction, multiple motors bind to a single actin filament and pull it against an external load, like people pulling on a rope in a tug-of-war. We model the dynamics of actomyosin filaments in order to study the evolution of motor-motor cooperativity. We find that filament backsliding-the distance an actin slides backward when a motor at the end of its cycle releases-is central to the speed and efficiency of muscle contraction. Our model predicts that this backsliding has been reduced through evolutionary adaptations to the motor's binding propensity, the strength of the motor's power stroke, and the force dependence of the motor's release from actin. These properties optimize the collective action of myosin II motors, which is not a simple sum of individual motor actions. The model also shows that these evolutionary variables can explain the speed-efficiency trade-off observed across different muscle tissues. This is an example of how evolution can tune the microscopic properties of individual proteins in order to optimize complex biological functions.
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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.