ArticleProceedings of the National Academy of Sciences of the United States of America2015
Knockout of Lmod2 results in shorter thin filaments followed by dilated cardiomyopathy and juvenile lethality.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 87 citations in OpenAlex.
- Transcriptomic adaptation during skeletal muscle habituation to eccentric or concentric exercise training.Scientific reports · 2021Trial
- A Combination of Alleles in LMOD2 and a lncRNA is Strongly Associated With Myxomatous Mitral Valve Disease in Cavalier King Charles Spaniels.Animal genetics · 2026Article
- 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
- 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
- Novel leiomodin 2b crispant zebrafish as a model for dilated cardiomyopathy.microPublication biology · 2026Article
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- LMOD2 interaction with ACTC1 regulates myogenic differentiation.BMC genomics · 2025Article
- Prediction and biological significance of small changes in binding of leiomodin to tropomyosin.The Journal of general physiology · 2025Article
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Interaction of cardiac leiomodin with the native cardiac thin filament.PLoS biology · 2025Article
- 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
- Leiomodin 2 neonatal dilated cardiomyopathy mutation results in altered actin gene signatures and cardiomyocyte dysfunction.NPJ Regenerative medicine · 2024Article
- Human disease-causing mutations result in loss of leiomodin 2 through nonsense-mediated mRNA decay.PLoS genetics · 2024Article
- Lmod2 is necessary for effective skeletal muscle contraction.Science advances · 2024Article
- 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
9 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
13 authors at 1 institution in 1 country.
Funding
Abstract
Leiomodin 2 (Lmod2) is an actin-binding protein that has been implicated in the regulation of striated muscle thin filament assembly; its physiological function has yet to be studied. We found that knockout of Lmod2 in mice results in abnormally short thin filaments in the heart. We also discovered that Lmod2 functions to elongate thin filaments by promoting actin assembly and dynamics at thin filament pointed ends. Lmod2-KO mice die as juveniles with hearts displaying contractile dysfunction and ventricular chamber enlargement consistent with dilated cardiomyopathy. Lmod2-null cardiomyocytes produce less contractile force than wild type when plated on micropillar arrays. Introduction of GFP-Lmod2 via adeno-associated viral transduction elongates thin filaments and rescues structural and functional defects observed in Lmod2-KO mice, extending their lifespan to adulthood. Thus, to our knowledge, Lmod2 is the first identified mammalian protein that functions to elongate actin filaments in the heart; it is essential for cardiac thin filaments to reach a mature length and is required for efficient contractile force and proper heart function during development.
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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.