ArticleThe Journal of biological chemistry2013
The superfast human extraocular myosin is kinetically distinct from the fast skeletal IIa, IIb, and IId isoforms.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Co-expression of MyHC-15 with other known isoforms in rat muscle spindles.European journal of histochemistry : EJH · 2025Article
- Protocols for Myosin and Actin-Myosin Assays Using Rapid, Stopped-Flow Kinetics.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Expression of MyHC-15 and -2x in human muscle spindles: An immunohistochemical study.Journal of anatomy · 2023Article
- Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Review
- Virus-free transfection, transient expression, and purification of human cardiac myosin in mammalian muscle cells for biochemical and biophysical assays.Scientific reports · 2023Article
- Alpha and beta myosin isoforms and human atrial and ventricular contraction.Cellular and molecular life sciences : CMLS · 2021Review
- Identification of sequence changes in myosin II that adjust muscle contraction velocity.PLoS biology · 2021Article
- Conformational distributions of isolated myosin motor domains encode their mechanochemical properties.eLife · 2020Article
- The ATPase cycle of human muscle myosin II isoforms: Adaptation of a single mechanochemical cycle for different physiological roles.The Journal of biological chemistry · 2019Article
- Atomistic Models from Orientation and Distance Constraints Using EPR of a Bifunctional Spin Label.Biophysical journal · 2019Article
- The load dependence of muscle's force-velocity curve is modulated by alternative myosin converter domains.American journal of physiology. Cell physiology · 2019Article
- Dilated cardiomyopathy myosin mutants have reduced force-generating capacity.The Journal of biological chemistry · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Five Alternative Myosin Converter Domains Influence Muscle Power, Stretch Activation, and Kinetics.Biophysical journal · 2018Article
- Fundamental constraints in synchronous muscle limit superfast motor control in vertebrates.eLife · 2017Article
- Modeling the Actin.myosin ATPase Cross-Bridge Cycle for Skeletal and Cardiac Muscle Myosin Isoforms.Biophysical journal · 2017Article
- Kinetic Adaptations of Myosins for Their Diverse Cellular Functions.Traffic (Copenhagen, Denmark) · 2016Review
- The Most Prevalent Freeman-Sheldon Syndrome Mutations in the Embryonic Myosin Motor Share Functional Defects.The Journal of biological chemistry · 2016Article
- Molecular determinants of force production in human skeletal muscle fibers: effects of myosin isoform expression and cross-sectional area.American journal of physiology. Cell physiology · 2015Article
- Global gene expression patterns of grass carp following compensatory growth.BMC genomics · 2015Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Humans express five distinct myosin isoforms in the sarcomeres of adult striated muscle (fast IIa, IId, the slow/cardiac isoform I/β, the cardiac specific isoform α, and the specialized extraocular muscle isoform). An additional isoform, IIb, is present in the genome but is not normally expressed in healthy human muscles. Muscle fibers expressing each isoform have distinct characteristics including shortening velocity. Defining the properties of the isoforms in detail has been limited by the availability of pure samples of the individual proteins. Here we study purified recombinant human myosin motor domains expressed in mouse C2C12 muscle cells. The results of kinetic analysis show that among the closely related adult skeletal isoforms, the affinity of ADP for actin·myosin (K(AD)) is the characteristic that most readily distinguishes the isoforms. The three fast muscle myosins have K(AD) values of 118, 80, and 55 μM for IId, IIa, and IIb, respectively, which follows the speed in motility assays from fastest to slowest. Extraocular muscle is unusually fast with a far weaker K(AD) = 352 μM. Sequence comparisons and homology modeling of the structures identify a few key areas of sequence that may define the differences between the isoforms, including a region of the upper 50-kDa domain important in signaling between the nucleotide pocket and the actin-binding site.
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