ArticleThe Journal of cell biology1989
The mechanism of assembly of Acanthamoeba myosin-II minifilaments: minifilaments assemble by three successive dimerization steps.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Reconstitution of actomyosin networks in cell-sized liposomes dissects distinct mechanisms of membrane blebbing and symmetry breaking.Science advances · 2026Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.Molecular biology of the cell · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.bioRxiv : the preprint server for biology · 2025Article
- SuggestingCells · 2024Article
- Non-muscle myosin 2 at a glance.Journal of cell science · 2023Review
- Dual-wavelength stopped-flow analysis of the lateral and longitudinal assembly kinetics of vimentin.Biophysical journal · 2022Article
- Bond Type and Discretization of Nonmuscle Myosin II Are Critical for Simulated Contractile Dynamics.Biophysical journal · 2020Article
- Unite to divide - how models and biological experimentation have come together to reveal mechanisms of cytokinesis.Journal of cell science · 2018Review
- Unified biophysical mechanism for cell-shape oscillations and cell ingression.Physical review. E · 2018Article
- Cross-linkers both drive and brake cytoskeletal remodeling and furrowing in cytokinesis.Molecular biology of the cell · 2018Article
- Structure of the fission yeast actomyosin ring during constriction.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Fission yeast myosin Myo2 is down-regulated in actin affinity by light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Actin dynamics and competition for myosin monomer govern the sequential amplification of myosin filaments.Nature cell biology · 2017Article
- Kinetic Monte Carlo simulations of the assembly of filamentous biomacromolecules by dimer addition mechanism.RSC advances · 2015Article
- A role for myosin II in mammalian mitochondrial fission.Current biology : CB · 2014Article
- Kinetic characterization of the ATPase and actin-activated ATPase activities of Acanthamoeba castellanii myosin-2.The Journal of biological chemistry · 2013Article
- Regulation of the actin-activated MgATPase activity of Acanthamoeba myosin II by phosphorylation of serine 639 in motor domain loop 2.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Regulation of the filament structure and assembly of Acanthamoeba myosin II by phosphorylation of serines in the heavy-chain nonhelical tailpiece.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Cytokinesis mechanics and mechanosensing.Cytoskeleton (Hoboken, N.J.) · 2012Review
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3 authors.
Funding
Abstract
We used 90 degrees light scattering, analytical ultracentrifugation, and electron microscopy to deduce that Acanthamoeba myosin-II minifilaments, composed of eight molecules each, assemble by a novel mechanism consisting of three successive dimerization steps rather than by the addition of monomers or parallel dimers to a nucleus. Above 200 mM KCl, Acanthamoeba myosin-II is monomeric. At low ionic strength (less than 100 mM KCl), myosin-II polymerizes into bipolar minifilaments. Between 100 and 200 mM KCl, plots of light scattering vs. myosin concentration all extrapolate to the origin but have slopes which decrease with increasing KCl. This indicates that structures intermediate in size between monomers and full length minifilaments are formed, and that the critical concentrations for assembly of these structures is very low. Analytical ultracentrifugation has confirmed that intermediate structures exist at these salt concentrations, and that they are in rapid equilibrium with each other. We believe these structures represent assembly intermediates and have used equilibrium analytical ultracentrifugation and electron microscopy to identify them. Polymerization begins with the formation of antiparallel dimers, with the two tails overlapping by approximately 15 nm. Two antiparallel dimers then associated with a 15-nm stagger to form an antiparallel tetramer. Finally, two tetramers associate with a 30-nm stagger to form the completed minifilament. At very low ionic strengths, the last step in the assembly mechanism is largely reversed and antiparallel tetramers are the predominant species. Alkaline pH, which can also induce minifilament disassembly, produces the same assembly intermediates as are found for salt induced disassembly.
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