ArticleThe Journal of biological chemistry2013
Characterization of three full-length human nonmuscle myosin II paralogs.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.
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Who cites it
137 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
- Binding of RbFox proteins at weak 5'splice site of A2 induces its alternative splicing in non-muscle myosin heavy-chain IIA mRNA.The Journal of biological chemistry · 2026Article
- Smooth muscle contractile cytoskeleton in health and disease.Journal of muscle research and cell motility · 2026Review
- Cryo-EM structure of shutdown human nonmuscle myosin 2A.Science advances · 2026Article
- MYH9 mutations differentially stabilize non-muscle myosin II filaments and induce distinct cellular aggregation phenotypes.Cellular and molecular life sciences : CMLS · 2026Article
- Intravital single-molecule imaging reveals cytoskeletal turnover as a driver of membrane remodeling in live animals.bioRxiv : the preprint server for biology · 2026Article
- Src-dependent tyrosine-phosphorylation of NM2A has a protective role against bacterial pore-forming toxins.PLoS pathogens · 2026Article
- A song of heads and tails: myosin II conformational regulation and filament dynamics shape force generation in non-muscle cells.Biophysical reviews · 2026Review
- Effect of Load on Non-Muscle Myosin 2 Paralog Filaments in a Biomimetic Contractile Actin Array.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- In Vitro Production of Full-Length Myosin 2 and Visualization of Actin Filament Motility by Total Internal Reflection Microscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mechanics of blunting of actin-myosin interaction dynamics by the actinopathy-causing mutation E334Q in cytoskeletal γ-actin.The Journal of physiology · 2026Article
- Phospho-activated non-muscle myosin IIA heavy chain supports different mechanisms of virus uptake.Journal of virology · 2025Article
- Myosin 2 drives actin contractility in fast-crawling species outside of the amorphean lineage.Current biology : CB · 2025Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025Article
- Myosin-9 is required for lysosome-mediated nonlytic reovirus egress.PLoS pathogens · 2025Article
- Nonmuscle myosin IIA (NMIIA) regulates anisotropic cell tension to maintain the hexagonal packing of mouse lens meridional row cells.Molecular biology of the cell · 2025Article
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Article
- Nonmuscle myosin 2 without an assembly competence domain can incorporate into established filaments in cells.Molecular biology of the cell · 2025Article
77 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
Nonmuscle myosin IIs (NM IIs) are a group of molecular motors involved in a wide variety of cellular processes including cytokinesis, migration, and control of cell morphology. There are three paralogs of the NM II heavy chain in humans (IIA, IIB, and IIC), each encoded by a separate gene. These paralogs are expressed at different levels according to cell type and have different roles and intracellular distributions in vivo. Most previous studies on NM II used tissue-purified protein or expressed fragments of the molecule, which presents potential drawbacks for characterizing individual paralogs of the intact protein in vitro. To circumvent current limitations and approach their native properties, we have successfully expressed and purified the three full-length human NM II proteins with their light chains, using the baculovirus/Sf9 system. The enzymatic and structural properties of the three paralogs were characterized. Although each NM II is capable of forming bipolar filaments, those formed by IIC tend to contain fewer constituent molecules than those of IIA and IIB. All paralogs adopt the compact conformation in the presence of ATP. Phosphorylation of the regulatory light chain leads to assembly into filaments, which bind to actin in the presence of ATP. The nature of interactions with actin filaments is shown with different paralogs exhibiting different actin binding behaviors under equivalent conditions. The data show that although NM IIA and IIB form filaments with similar properties, NM IIC forms filaments that are less well suited to roles such as tension maintenance within the cell.
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