ArticleProceedings of the National Academy of Sciences of the United States of America2020
Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 13 citations in OpenAlex.
- Cancer Cell-Derived Small Extracellular Vesicles Are Associated with Impaired C2C12 Myoblast Differentiation.International journal of molecular sciences · 2026Article
- Nonmuscle myosin 2 without an assembly competence domain can incorporate into established filaments in cells.Molecular biology of the cell · 2025Article
- Local monomer levels and established filaments potentiate non-muscle myosin 2 assembly.The Journal of cell biology · 2024Article
- SuggestingCells · 2024Article
- Myosin assembly of smooth muscle: from ribbons and side polarity to a row polar helical model.Journal of muscle research and cell motility · 2022Article
- Comparative Transcriptome Sequencing Analysis ofFrontiers in physiology · 2022Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
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3 authors at 1 institution in 1 country.
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Abstract
Muscle contraction depends on the cyclical interaction of myosin and actin filaments. Therefore, it is important to understand the mechanisms of polymerization and depolymerization of muscle myosins. Muscle myosin 2 monomers exist in two states: one with a folded tail that interacts with the heads (10S) and one with an unfolded tail (6S). It has been thought that only unfolded monomers assemble into bipolar and side-polar (smooth muscle myosin) filaments. We now show by electron microscopy that, after 4 s of polymerization in vitro in both the presence (smooth muscle myosin) and absence of ATP, skeletal, cardiac, and smooth muscle myosins form tail-folded monomers without tail-head interaction, tail-folded antiparallel dimers, tail-folded antiparallel tetramers, unfolded bipolar tetramers, and small filaments. After 4 h, the myosins form thick bipolar and, for smooth muscle myosin, side-polar filaments. Nonphosphorylated smooth muscle myosin polymerizes in the presence of ATP but with a higher critical concentration than in the absence of ATP and forms only bipolar filaments with bare zones. Partial depolymerization in vitro of nonphosphorylated smooth muscle myosin filaments by the addition of MgATP is the reverse of polymerization.
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