ReviewBiophysical journal2017
Tropomodulins and Leiomodins: Actin Pointed End Caps and Nucleators in Muscles.
Review in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
63 citing papers in PubMed, 80 citations in OpenAlex.
- Loss of the Coronary Artery Disease Risk GeneCirculation · 2026Article
- Article
- Leiomodin2 is a polymerase at the pointed ends of actin filaments.Nature communications · 2026Article
- Mechanism of actin thin filament pointed-end elongation by leiomodin.Nature communications · 2026Article
- Leiomodin 2 is a processive pointed-end elongator of actin filaments.Nature communications · 2026Article
- Localization and functional exploration of leiomodin-2's C-terminal binding sites.Biochimica et biophysica acta. Proteins and proteomics · 2026Article
- Leiomodin 2 functions as a processive pointed-end elongator of actin filaments.bioRxiv : the preprint server for biology · 2026Article
- N-Terminal Actin-Binding Site of Lmod2 Promotes Controlled Pointed End Elongation.Circulation research · 2026Article
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Sex-specific phosphoproteome responses to calorie restriction and insulin in skeletal muscle from older rats.The journals of gerontology. Series A, Biological sciences and medical sciences · 2025Article
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Prediction and biological significance of small changes in binding of leiomodin to tropomyosin.The Journal of general physiology · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Interaction of cardiac leiomodin with the native cardiac thin filament.PLoS biology · 2025Article
- Reconstitution of Arp2/3-nucleated actin assembly with proteins CP, V-1, and CARMIL.Current biology : CB · 2024Article
- Dilated cardiomyopathy-associated skeletal muscle actin (ACTA1) mutation R256H disrupts actin structure and function and causes cardiomyocyte hypocontractility.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy.Science advances · 2024Article
- Reconstitution of Arp2/3-Nucleated Actin Assembly with CP, V-1 and CARMIL.bioRxiv : the preprint server for biology · 2024Article
- Recessive TMOD1 mutation causes childhood cardiomyopathy.Communications biology · 2024Article
- Peripheral thickening of the sarcomeres and pointed end elongation of the thin filaments are both promoted by SALS and its formin interaction partners.PLoS genetics · 2024Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Cytoskeletal structures characterized by actin filaments with uniform lengths, including the thin filaments of striated muscles and the spectrin-based membrane skeleton, use barbed and pointed-end capping proteins to control subunit addition/dissociation at filament ends. While several proteins cap the barbed end, tropomodulins (Tmods), a family of four closely related isoforms in vertebrates, are the only proteins known to specifically cap the pointed end. Tmods are ∼350 amino acids in length, and comprise alternating tropomyosin- and actin-binding sites (TMBS1, ABS1, TMBS2, and ABS2). Leiomodins (Lmods) are related in sequence to Tmods, but display important differences, including most notably the lack of TMBS2 and the presence of a C-terminal extension featuring a proline-rich domain and an actin-binding WASP-Homology 2 domain. The Lmod subfamily comprises three somewhat divergent isoforms expressed predominantly in muscle cells. Biochemically, Lmods differ from Tmods, acting as powerful nucleators of actin polymerization, not capping proteins. Structurally, Lmods and Tmods display crucial differences that correlate well with their different biochemical activities. Physiologically, loss of Lmods in striated muscle results in cardiomyopathy or nemaline myopathy, whereas complete loss of Tmods leads to failure of myofibril assembly and developmental defects. Yet, interpretation of some of the in vivo data has led to the idea that Tmods and Lmods are interchangeable or, at best, different variants of two subfamilies of pointed-end capping proteins. Here, we review and contrast the existing literature on Tmods and Lmods, and propose a model of Lmod function that attempts to reconcile the in vitro and in vivo data, whereby Lmods nucleate actin filaments that are subsequently capped by Tmods during sarcomere assembly, turnover, and repair.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.