ArticleProceedings of the National Academy of Sciences of the United States of America2018
Polymerization pathway of mammalian nonmuscle myosin 2s.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Role of the nonhelical tailpiece of myosin-II in regulating filament architecture and function.The Journal of cell biology · 2026Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.Nature communications · 2026Article
- Src-dependent tyrosine-phosphorylation of NM2A has a protective role against bacterial pore-forming toxins.PLoS pathogens · 2026Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025Article
- Nonmuscle myosin 2 without an assembly competence domain can incorporate into established filaments in cells.Molecular biology of the cell · 2025Article
- Myosin 2 - A general contractor for the cytoskeleton.Current opinion in cell biology · 2025Review
- Drebrin is Required for Myosin-facilitated Actin Cytoskeletal Remodeling during Pulmonary Alveolar Development.American journal of respiratory cell and molecular biology · 2024Article
- SuggestingCells · 2024Article
- Synaptopodin stress fiber and contractomere at the epithelial junction.The Journal of cell biology · 2022Article
- Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021Review
- Antibodies in cerebral cavernous malformations react with cytoskeleton autoantigens in the lesional milieu.Journal of autoimmunity · 2020Observational
- Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Comparative Analysis of the Roles of Non-muscle Myosin-IIs in Cytokinesis in Budding Yeast, Fission Yeast, and Mammalian Cells.Frontiers in cell and developmental biology · 2020Review
- Network Contractility During Cytokinesis-from Molecular to Global Views.Biomolecules · 2019Review
- Common and Specific Functions of Nonmuscle Myosin II Paralogs in Cells.Biochemistry. Biokhimiia · 2018Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three mammalian nonmuscle myosin 2 (NM2) monomers, like all class 2 myosin monomers, are hexamers of two identical heavy (long) chains and two pairs of light (short) chains bound to the heavy chains. The heavy chains have an N-terminal globular motor domain (head) with actin-activated ATPase activity, a lever arm (neck) to which the two light chains bind, and a coiled-coil helical tail. Monomers polymerize into bipolar filaments, with globular heads at each end separated by a bare zone, by antiparallel association of their coiled-coil tails. NM2 filaments are highly dynamic in situ, frequently disassembling and reassembling at different locations within the cell where they are essential for multiple biological functions. Therefore, it is important to understand the mechanisms of filament polymerization and depolymerization. Monomers can exist in two states: folded and unfolded. It has been thought that unfolded monomers form antiparallel dimers that assemble into bipolar filaments. We now show that polymerization in vitro proceeds from folded monomers to folded antiparallel dimers to folded antiparallel tetramers that unfold forming antiparallel bipolar tetramers. Folded dimers and tetramers then associate with the unfolded tetramer and unfold, forming a mature bipolar filament consisting of multiple unfolded tetramers with an entwined bare zone. We also demonstrate that depolymerization is essentially the reverse of the polymerization process. These results will advance our understanding of NM2 filament dynamics in situ.
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