ArticleBiophysical journal2013
Thick filament length and isoform composition determine self-organized contractile units in actomyosin bundles.
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 40 papers.
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40 citing papers in PubMed, 77 citations in OpenAlex.
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- Myosin and [Formula: see text]-actinin regulation of stress fiber contractility under tensile stress.Scientific reports · 2023Article
- Jamming Transitions in Astrocytes and Glioblastoma Are Induced by Cell Density and Tension.Cells · 2022Article
- F-actin architecture determines constraints on myosin thick filament motion.Nature communications · 2022Article
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- Actin bundle architecture and mechanics regulate myosin II force generation.Biophysical journal · 2021Article
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- The Actin Cytoskeleton as an Active Adaptive Material.Annual review of condensed matter physics · 2020Article
- Large and reversible myosin-dependent forces in rigidity sensing.Nature physics · 2019Article
- Self-organizing motors divide active liquid droplets.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Architectural Dynamics of CaMKII-Actin Networks.Biophysical journal · 2019Article
- Ultrafast epithelial contractions provide insights into contraction speed limits and tissue integrity.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- UNC-45a promotes myosin folding and stress fiber assembly.The Journal of cell biology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Diverse myosin II isoforms regulate contractility of actomyosin bundles in disparate physiological processes by variations in both motor mechanochemistry and the extent to which motors are clustered into thick filaments. Although the role of mechanochemistry is well appreciated, the extent to which thick filament length regulates actomyosin contractility is unknown. Here, we study the contractility of minimal actomyosin bundles formed in vitro by mixtures of F-actin and thick filaments of nonmuscle, smooth, and skeletal muscle myosin isoforms with varied length. Diverse myosin II isoforms guide the self-organization of distinct contractile units within in vitro bundles with shortening rates similar to those of in vivo myofibrils and stress fibers. The tendency to form contractile units increases with the thick filament length, resulting in a bundle shortening rate proportional to the length of constituent myosin thick filament. We develop a model that describes our data, providing a framework in which to understand how diverse myosin II isoforms regulate the contractile behaviors of disordered actomyosin bundles found in muscle and nonmuscle cells. These experiments provide insight into physiological processes that use dynamic regulation of thick filament length, such as smooth muscle contraction.
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