ArticleThe Journal of biological chemistry2013
Kinetic characterization of nonmuscle myosin IIb at the single molecule level.
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 54 papers.
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Who cites it
54 citing papers in PubMed, 74 citations in OpenAlex.
- Effect of Load on Non-Muscle Myosin 2 Paralog Filaments in a Biomimetic Contractile Actin Array.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Three types of actomyosin rings within a common cytoplasm exhibit distinct modes of contractility.bioRxiv : the preprint server for biology · 2025Article
- Article
- Expression, Purification, and In Vitro Analysis of Myosin.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Non-Muscle Myosin II A: Friend or Foe in Cancer?International journal of molecular sciences · 2024Review
- Myosin-induced F-actin fragmentation facilitates contraction of actin networks.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Nonmuscle myosin 2 filaments are processive in cells.Biophysical journal · 2023Article
- Contractile ring composition dictates kinetics of in silico contractility.Biophysical journal · 2023Article
- Cingulin and paracingulin tether myosins-2 to junctions to mechanoregulate the plasma membrane.The Journal of cell biology · 2023Article
- Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023Article
- Synaptopodin stress fiber and contractomere at the epithelial junction.The Journal of cell biology · 2022Article
- Calponin 1 contributes to myofibroblast differentiation of human pleural mesothelial cells.American journal of physiology. Lung cellular and molecular physiology · 2022Article
- Functional Role of Non-Muscle Myosin II in Microglia: An Updated Review.International journal of molecular sciences · 2021Review
- The formin inhibitor SMIFH2 inhibits members of the myosin superfamily.Journal of cell science · 2021Article
- Evidence for S2 flexibility by direct visualization of quantum dot-labeled myosin heads and rods within smooth muscle myosin filaments moving on actin in vitro.The Journal of general physiology · 2021Article
- Review
- Bond Type and Discretization of Nonmuscle Myosin II Are Critical for Simulated Contractile Dynamics.Biophysical journal · 2020Article
- Conformational distributions of isolated myosin motor domains encode their mechanochemical properties.eLife · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Nonmuscle myosin IIB (NMIIB) is a cytoplasmic myosin, which plays an important role in cell motility by maintaining cortical tension. It forms bipolar thick filaments with ~14 myosin molecule dimers on each side of the bare zone. Our previous studies showed that the NMIIB is a moderately high duty ratio (~20-25%) motor. The ADP release step (~0.35 s(-1)) of NMIIB is only ~3 times faster than the rate-limiting phosphate release (0.13 ± 0.01 s(-1)). The aim of this study was to relate the known in vitro kinetic parameters to the results of single molecule experiments and to compare the kinetic and mechanical properties of single- and double-headed myosin fragments and nonmuscle IIB thick filaments. Examination of the kinetics of NMIIB interaction with actin at the single molecule level was accomplished using total internal reflection fluorescence (TIRF) with fluorescence imaging with 1-nm accuracy (FIONA) and dual-beam optical trapping. At a physiological ATP concentration (1 mm), the rate of detachment of the single-headed and double-headed molecules was similar (~0.4 s(-1)). Using optical tweezers we found that the power stroke sizes of single- and double-headed heavy meromyosin (HMM) were each ~6 nm. No signs of processive stepping at the single molecule level were observed in the case of NMIIB-HMM in optical tweezers or TIRF/in vitro motility experiments. In contrast, robust motility of individual fluorescently labeled thick filaments of full-length NMIIB was observed on actin filaments. Our results are in good agreement with the previous steady-state and transient kinetic studies and show that the individual nonprocessive nonmuscle myosin IIB molecules form a highly processive unit when polymerized into filaments.
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