ArticleThe Journal of cell biology1993
Tropomodulin is associated with the free (pointed) ends of the thin filaments in rat skeletal muscle.
Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 154 citations in OpenAlex.
- Review
- Mutual dependence between tropomodulin and tropomyosin in the regulation of sarcomeric actin assembly in Caenorhabditis elegans striated muscle.European journal of cell biology · 2022Article
- Thick filament-associated myosin undergoes frequent replacement at the tip of the thick filament.FEBS open bio · 2022Article
- Heterozygous Tropomodulin 3 mice have improved lung vascularization after chronic hypoxia.Human molecular genetics · 2022Article
- Dia- and Rok-dependent enrichment of capping proteins in a cortical region.Journal of cell science · 2021Article
- Quantitative high-precision imaging of myosin-dependent filamentous actin dynamics.Journal of muscle research and cell motility · 2020Review
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- Multifunctional roles of tropomodulin-3 in regulating actin dynamics.Biophysical reviews · 2018Review
- Tropomodulin Isoform-Specific Regulation of Dendrite Development and Synapse Formation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018Article
- Cardiac-specific knockout of Lmod2 results in a severe reduction in myofilament force production and rapid cardiac failure.Journal of molecular and cellular cardiology · 2018Article
- Characterizing interaction forces between actin and proteins of the tropomodulin family reveals the presence of the N-terminal actin-binding site in leiomodin.Archives of biochemistry and biophysics · 2018Article
- Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells.Molecular biology of the cell · 2017Article
- A Third Look at the Structure of Leiomodin Bound to Actin.Biophysical journal · 2017Article
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- Software-based measurement of thin filament lengths: an open-source GUI for Distributed Deconvolution analysis of fluorescence images.Journal of microscopy · 2017Article
- Apical Sarcomere-like Actomyosin Contracts Nonmuscle Drosophila Epithelial Cells.Developmental cell · 2016Article
- Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle.Development (Cambridge, England) · 2015Article
- Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethality.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Myosin motor isoforms direct specification of actomyosin function by tropomyosins.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Loss of Tropomodulin4 in the zebrafish mutant träge causes cytoplasmic rod formation and muscle weakness reminiscent of nemaline myopathy.Disease models & mechanisms · 2014Article
1 more citing papers are in PubMed but not listed here.
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The length and spatial organization of thin filaments in skeletal muscle sarcomeres are precisely maintained and are essential for efficient muscle contraction. While the major structural components of skeletal muscle sarcomeres have been well characterized, the mechanisms that regulate thin filament length and spatial organization are not well understood. Tropomodulin is a new, 40.6-kD tropomyosin-binding protein from the human erythrocyte membrane skeleton that binds to one end of erythrocyte tropomyosin and blocks head-to-tail association of tropomyosin molecules along actin filaments. Here we show that rat psoas skeletal muscle contains tropomodulin based on immunoreactivity, identical apparent mobility on SDS gels, and ability to bind muscle tropomyosin. Results from immunofluorescence labeling of isolated myofibrils at resting and stretched lengths using anti-erythrocyte tropomodulin antibodies indicate that tropomodulin is localized at or near the free (pointed) ends of the thin filaments; this localization is not dependent on the presence of myosin thick filaments. Immunoblotting of supernatants and pellets obtained after extraction of myosin from myofibrils also indicates that tropomodulin remains associated with the thin filaments. 1.2-1.6 copies of muscle tropomodulin are present per thin filament in myofibrils, supporting the possibility that one or two tropomodulin molecules may be associated with the two terminal tropomyosin molecules at the pointed end of each thin filament. Although a number of proteins are associated with the barbed ends of the thin filaments at the Z disc, tropomodulin is the first protein to be specifically located at or near the pointed ends of the thin filaments. We propose that tropomodulin may cap the tropomyosin polymers at the pointed end of the thin filament and play a role in regulating thin filament length.
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