ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2018
Ordering of myosin II filaments driven by mechanical forces: experiments and theory.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- MYH9 mutations differentially stabilize non-muscle myosin II filaments and induce distinct cellular aggregation phenotypes.Cellular and molecular life sciences : CMLS · 2026Article
- Research progress on the function of non-muscle myosin II during cell division.Frontiers in cell and developmental biology · 2026Review
- Article
- MYL1-Related Congenital Myopathy: Clinical, Genetic and Pathological Insights.Neuropathology and applied neurobiology · 2025Article
- Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024Review
- Massive field-of-view sub-cellular traction force videography enabled by Single-Pixel Optical Tracers (SPOT).Biosensors & bioelectronics · 2024Article
- Optimal mechanical interactions direct multicellular network formation on elastic substrates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Isoform selectivities of novel 4-hydroxycoumarin imines as inhibitors of myosin II.European journal of medicinal chemistry · 2023Article
- Scratching beyond the surface - minimal actin assemblies as tools to elucidate mechanical reinforcement and shape change.Emerging topics in life sciences · 2022Article
- A comprehensive review of computational and image analysis techniques for quantitative evaluation of striated muscle tissue architecture.Biophysics reviews · 2022Review
- Article
- Identification of crucial circRNAs in skeletal muscle during chicken embryonic development.BMC genomics · 2022Article
- Rbfox1 is required for myofibril development and maintaining fiber type-specific isoform expression inLife science alliance · 2022Article
- Article
- Article
- Modeling mechanochemical pattern formation in elastic sheets of biological matter.The European physical journal. E, Soft matter · 2021Article
- Matrix Stiffness Modulates Mechanical Interactions and Promotes Contact between Motile Cells.Biomedicines · 2021Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
Corrections and comments
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Authors and funding
5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Myosin II filaments form ordered superstructures in both cross-striated muscle and non-muscle cells. In cross-striated muscle, myosin II (thick) filaments, actin (thin) filaments and elastic titin filaments comprise the stereotypical contractile units of muscles called sarcomeres. Linear chains of sarcomeres, called myofibrils, are aligned laterally in registry to form cross-striated muscle cells. The experimentally observed dependence of the registered organization of myofibrils on extracellular matrix elasticity has been proposed to arise from the interactions of sarcomeric contractile elements (considered as force dipoles) through the matrix. Non-muscle cells form small bipolar filaments built of less than 30 myosin II molecules. These filaments are associated in registry forming superstructures ('stacks') orthogonal to actin filament bundles. Formation of myosin II filament stacks requires the myosin II ATPase activity and function of the actin filament crosslinking, polymerizing and depolymerizing proteins. We propose that the myosin II filaments embedded into elastic, intervening actin network (IVN) function as force dipoles that interact attractively through the IVN. This is in analogy with the theoretical picture developed for myofibrils where the elastic medium is now the actin cytoskeleton itself. Myosin stack formation in non-muscle cells provides a novel mechanism for the self-organization of the actin cytoskeleton at the level of the entire cell.This article is part of the theme issue 'Self-organization in cell biology'.
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