ArticleThe Journal of biological chemistry2011
Comparative kinetic and functional characterization of the motor domains of human nonmuscle myosin-2C isoforms.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 61 citations in OpenAlex.
- 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
- Article
- MYH9 mutations differentially stabilize non-muscle myosin II filaments and induce distinct cellular aggregation phenotypes.Cellular and molecular life sciences : CMLS · 2026Article
- Uncovering the genetic architecture of ME/CFS: a precision approach reveals impact of rare monogenic variation.Journal of translational medicine · 2025Article
- Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.bioRxiv : the preprint server for biology · 2025Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Article
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- Structural insights into actin isoforms.eLife · 2023Article
- Unique and redundant functions of cytoplasmic actins and nonmuscle myosin II isoforms at epithelial junctions.Annals of the New York Academy of Sciences · 2022Review
- Mapping drug-target interactions and synergy in multi-molecular therapeutics for pressure-overload cardiac hypertrophy.NPJ systems biology and applications · 2021Article
- Nonmuscle myosin-2 contractility-dependent actin turnover limits the length of epithelial microvilli.Molecular biology of the cell · 2020Article
- Review
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Converter domain mutations in myosin alter structural kinetics and motor function.The Journal of biological chemistry · 2019Article
- Mammalian nonmuscle myosin II comes in three flavors.Biochemical and biophysical research communications · 2018Review
- Myosin-IIA heavy chain phosphorylation on S1943 regulates tumor metastasis.Experimental cell research · 2018Article
- Replacing nonmuscle myosin 2A with myosin 2C1 permits gastrulation but not placenta vascular development in mice.Molecular biology of the cell · 2018Article
- Bipolar filaments of human nonmuscle myosin 2-A and 2-B have distinct motile and mechanical properties.eLife · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonmuscle myosins are widely distributed and play important roles in the maintenance of cell morphology and cytokinesis. In this study, we compare the detailed kinetic and functional characterization of naturally occurring transcript variants of the motor domain of human nonmuscle myosin heavy chain (NMHC)-2C. NMHC-2C is alternatively spliced both in loop-1 and loop-2. Isoform 2C0 contains no inserts in either of the loops and represents the shortest isoform. An 8-amino acid extension in the loop-1 region is present in isoforms 2C1 and 2C1C2. Isoform 2C1C2 additionally displays a 33-amino acid extension in the loop-2 region. Transient kinetic experiments indicate increased rate constants for F-actin binding by isoform 2C1C2 in the absence and presence of nucleotide, which can be attributed to the loop-2 extension. ADP binding shows only minor differences for the three transcript variants. In contrast, larger differences are observed for the rates of ADP release both in the absence and presence of F-actin. The largest differences are observed between isoforms 2C0 and 2C1C2. In the absence and presence of F-actin, isoform 2C1C2 displays a 5-7-fold increase in ADP affinity. Moreover, our results indicate that the ADP release kinetics of all three isoforms are modulated by changes in the concentration of free Mg(2+) ions. The greatest responsiveness of the NMHC-2C isoforms is observed in the physiological range from 0.2 to 1.5 mM free Mg(2+) ions, affecting their duty ratio, velocity, and tension-bearing properties.
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