ArticleThe Journal of biological chemistry2010
Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 61 citations in OpenAlex.
- SH3BGRL proteins are thioredoxin fold-containing actin filament pointed end capping proteins (TPECs).Scientific reports · 2026Article
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Integrated structural model of the palladin-actin complex using XL-MS, docking, NMR, and SAXS.Protein science : a publication of the Protein Society · 2025Article
- Tropomodulin1 exacerbates inflammatory response in macrophages by negatively regulating LPS-induced TLR4 endocytosis.Cellular and molecular life sciences : CMLS · 2024Article
- Article
- Effects of Tropomodulin 2 on Dendritic Spine Reorganization and Dynamics.Biomolecules · 2023Article
- Drosophila Tropomodulin is required for multiple actin-dependent processes within developing myofibers.Development (Cambridge, England) · 2023Article
- Tmod3 Phosphorylation Mediates AMPK-Dependent GLUT4 Plasma Membrane Insertion in Myoblasts.Frontiers in endocrinology · 2021Article
- Tropomodulin1 Expression Increases Upon Maturation in Dendritic Cells and Promotes Their Maturation and Immune Functions.Frontiers in immunology · 2020Article
- 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
- 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
- Tropomodulin's Actin-Binding Abilities Are Required to Modulate Dendrite Development.Frontiers in molecular neuroscience · 2018Article
- HSPB7 is indispensable for heart development by modulating actin filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Molecular and cellular neurosciences · 2017Review
- Tropomodulin 1 controls erythroblast enucleation via regulation of F-actin in the enucleosome.Blood · 2017Article
- Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.Biophysical journal · 2017Review
- Roles of actin binding proteins in mammalian oocyte maturation and beyond.Cell cycle (Georgetown, Tex.) · 2016Review
- Tropomyosin-binding properties modulate competition between tropomodulin isoforms.Archives of biochemistry and biophysics · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Many actin-binding proteins have been shown to possess multiple activities to regulate filament dynamics. Tropomodulins (Tmod1-4) are a conserved family of actin filament pointed end-capping proteins. Our previous work has demonstrated that Tmod3 binds to monomeric actin in addition to capping pointed ends. Here, we show a novel actin-nucleating activity in mammalian Tmods. Comparison of Tmod isoforms revealed that Tmod1-3 but not Tmod4 nucleate actin filament assembly. All Tmods bind to monomeric actin, and Tmod3 forms a 1:1 complex with actin. By truncation and mutagenesis studies, we demonstrated that the second α-helix in the N-terminal domain of Tmod3 is essential for actin monomer binding. Chemical cross-linking and LC-MS/MS further indicated that residues in this second α-helix interact with actin subdomain 2, whereas Tmod3 N-terminal domain peptides distal to this α-helix interact with actin subdomain 1. Mutagenesis of Leu-73 to Asp, which disrupts the second α-helix of Tmod3, decreases both its actin monomer-binding and -nucleating activities. On the other hand, point mutations of residues in the C-terminal leucine-rich repeat domain of Tmod3 (Lys-317 in the fifth leucine-rich repeat β-sheet and Lys-344 or Arg-345/Arg-346 in the C-terminal α6-helix) significantly reduced pointed end-capping and nucleation without altering actin monomer binding. Taken together, our data indicate that Tmod3 binds actin monomers over an extended interface and that nucleating activity depends on actin monomer binding and pointed end-capping activities, contributed by N- and C-terminal domains of Tmod3, respectively. Tmod3 nucleation of actin assembly may regulate the cytoskeleton in dynamic cellular contexts.
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