ArticleThe Journal of biological chemistry2011
Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes.
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 30 papers.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Recessive TMOD1 mutation causes childhood cardiomyopathy.Communications biology · 2024Article
- A nemaline myopathy-linked mutation inhibits the actin-regulatory functions of tropomodulin and leiomodin.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- A human FLII gene variant alters sarcomeric actin thin filament length and predisposes to cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Tmod3 Phosphorylation Mediates AMPK-Dependent GLUT4 Plasma Membrane Insertion in Myoblasts.Frontiers in endocrinology · 2021Article
- Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.PLoS biology · 2020Article
- Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.Journal of muscle research and cell motility · 2020Review
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Molecular and cellular neurosciences · 2017Review
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.PloS one · 2017Article
- The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2's function.Molecular biology of the cell · 2016Article
- Tropomyosin-binding properties modulate competition between tropomodulin isoforms.Archives of biochemistry and biophysics · 2016Article
- Tropomodulin isoforms utilize specific binding functions to modulate dendrite development.Cytoskeleton (Hoboken, N.J.) · 2016Article
- Localization of the binding interface between leiomodin-2 and α-tropomyosin.Biochimica et biophysica acta · 2016Article
- The Role of Leucine-Rich Repeat Containing Protein 10 (LRRC10) in Dilated Cardiomyopathy.Frontiers in physiology · 2016Review
- How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.Nature communications · 2015Article
- Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis.Journal of cell science · 2015Article
- Tropomodulin3 is a novel Akt2 effector regulating insulin-stimulated GLUT4 exocytosis through cortical actin remodeling.Nature communications · 2015Article
- Mechanism of actin filament pointed-end capping by tropomodulin.Science (New York, N.Y.) · 2014Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Tropomodulin is a tropomyosin-dependent actin filament capping protein involved in the structural formation of thin filaments and in the regulation of their lengths through its localization at the pointed ends of actin filaments. The disordered N-terminal domain of tropomodulin contains three functional sites: two tropomyosin-binding and one tropomyosin-dependent actin-capping sites. The C-terminal half of tropomodulin consists of one compact domain containing a tropomyosin-independent actin-capping site. Here we determined the structural properties of tropomodulin-1 that affect its roles in cardiomyocytes. To explore the significance of individual tropomyosin-binding sites, GFP-tropomodulin-1 with single mutations that destroy each tropomyosin-binding site was expressed in cardiomyocytes. We demonstrated that both sites are necessary for the optimal localization of tropomodulin-1 at thin filament pointed ends, with site 2 acting as the major determinant. To investigate the functional properties of the tropomodulin C-terminal domain, truncated versions of GFP-tropomodulin-1 were expressed in cardiomyocytes. We discovered that the leucine-rich repeat (LRR) fold and the C-terminal helix are required for its proper targeting to the pointed ends. To investigate the structural significance of the LRR fold, we generated three mutations within the C-terminal domain (V232D, F263D, and L313D). Our results show that these mutations affect both tropomyosin-independent actin-capping activity and pointed end localization, most likely by changing local conformations of either loops or side chains of the surfaces involved in the interactions of the LRR domain. Studying the influence of these mutations individually, we concluded that, in addition to the tropomyosin-independent actin-capping site, there appears to be another regulatory site within the tropomodulin C-terminal domain.
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