ArticleNature communications2015
How Leiomodin and Tropomodulin use a common fold for different actin assembly functions.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Loss of the Coronary Artery Disease Risk GeneCirculation · 2026Article
- Article
- 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
- Interaction of cardiac leiomodin with the native cardiac thin filament.PLoS biology · 2025Article
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy.Science advances · 2024Article
- Lmod2 is necessary for effective skeletal muscle contraction.Science advances · 2024Article
- Gene expression in notochord and nuclei pulposi: a study of gene families across the chordate phylum.BMC ecology and evolution · 2023Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- CaProtein science : a publication of the Protein Society · 2022Article
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Actin-Associated Proteins and Small Molecules Targeting the Actin Cytoskeleton.International journal of molecular sciences · 2022Review
- Genetic dissection of novel myopathy models reveals a role of CapZα and Leiomodin 3 during myofibril elongation.PLoS genetics · 2022Article
- Review
- Novel insights into sarcomere regulatory systems control of cardiac thin filament activation.The Journal of general physiology · 2021Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
How proteins sharing a common fold have evolved different functions is a fundamental question in biology. Tropomodulins (Tmods) are prototypical actin filament pointed-end-capping proteins, whereas their homologues, Leiomodins (Lmods), are powerful filament nucleators. We show that Tmods and Lmods do not compete biochemically, and display similar but distinct localization in sarcomeres. Changes along the polypeptide chains of Tmods and Lmods exquisitely adapt their functions for capping versus nucleation. Tmods have alternating tropomyosin (TM)- and actin-binding sites (TMBS1, ABS1, TMBS2 and ABS2). Lmods additionally contain a C-terminal extension featuring an actin-binding WH2 domain. Unexpectedly, the different activities of Tmods and Lmods do not arise from the Lmod-specific extension. Instead, nucleation by Lmods depends on two major adaptations-the loss of pointed-end-capping elements present in Tmods and the specialization of the highly conserved ABS2 for recruitment of two or more actin subunits. The WH2 domain plays only an auxiliary role in nucleation.
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