ArticleThe Journal of cell biology1989
The effect of heavy chain phosphorylation and solution conditions on the assembly of Acanthamoeba myosin-II.
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 23 papers.
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Who cites it
23 citing papers in PubMed.
- SuggestingCells · 2024Article
- 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
- Emergent mechanics of actomyosin drive punctuated contractions and shape network morphology in the cell cortex.PLoS computational biology · 2018Article
- Fission yeast Myo2: Molecular organization and diffusion in the cytoplasm.Cytoskeleton (Hoboken, N.J.) · 2018Article
- 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
- 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
- Myosin filament assembly requires a cluster of four positive residues located in the rod domain.FEBS letters · 2012Article
- Mutations at the same amino acid in myosin that cause either skeletal or cardiac myopathy have distinct molecular phenotypes.Journal of molecular and cellular cardiology · 2010Article
- Mutations in the beta-myosin rod cause myosin storage myopathy via multiple mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Non-muscle myosin-II-B filament regulation of paracellular resistance in cervical epithelial cells is associated with modulation of the cortical acto-myosin.Journal of the Society for Gynecologic Investigation · 2006Article
- Estrogen regulates epithelial cell deformability by modulation of cortical actomyosin through phosphorylation of nonmuscle myosin heavy-chain II-B filaments.Endocrinology · 2006Article
- Differential requirement for the nonhelical tailpiece and the C terminus of the myosin rod in Caenorhabditis elegans muscle.Molecular biology of the cell · 2003Article
- Myosin-II tails confer unique functions in Schizosaccharomyces pombe: characterization of a novel myosin-II tail.Molecular biology of the cell · 2000Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- Non-sarcomeric mode of myosin II organization in the fibroblast lamellum.The Journal of cell biology · 1993Article
- Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.The Journal of cell biology · 1992Article
- Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin-II.Journal of muscle research and cell motility · 1991Article
- Characterization of actin filament severing by actophorin from Acanthamoeba castellanii.The Journal of cell biology · 1991Article
- Identification of functional regions on the tail of Acanthamoeba myosin-II using recombinant fusion proteins. I. High resolution epitope mapping and characterization of monoclonal antibody binding sites.The Journal of cell biology · 1990Article
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2 authors.
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Abstract
At low ionic strength, Acanthamoeba myosin-II polymerizes into bipolar minifilaments, consisting of eight molecules, that scatter about three times as much light as monomers. With this light scattering assay, we show that the critical concentration for assembly in 50-mM KCl is less than 5 nM. Phosphorylation of the myosin heavy chain over the range of 0.7 to 3.7 P per molecule has no effect on its KCl dependent assembly properties: the structure of the filaments, the extent of assembly, and the critical concentration for assembly are the same. Sucrose at a concentration above a few percent inhibits polymerization. Millimolar concentrations of MgCl2 induce the lateral aggregation of fully formed minifilaments into thick filaments. Compared with dephosphorylated minifilaments, minifilaments of phosphorylated myosin have a lower tendency to aggregate laterally and require higher concentrations of MgCl2 for maximal light scattering. Acidic pH also induces lateral aggregation, whereas basic pH leads to depolymerization of the myosin-II minifilaments. Under polymerizing conditions, millimolar concentrations of ATP only slightly decrease the light scattering of either phosphorylated or dephosphorylated myosin-II. Barring further modulation of assembly by unknown proteins, both phosphorylated and dephosphorylated myosin-II are expected to be in the form of minifilaments under the ionic conditions existing within Acanthamoeba.
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