ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- N-Terminal Actin-Binding Site of Lmod2 Promotes Controlled Pointed End Elongation.Circulation research · 2026Article
- Interaction of cardiac leiomodin with the native cardiac thin filament.PLoS biology · 2025Article
- Leiomodin 2 neonatal dilated cardiomyopathy mutation results in altered actin gene signatures and cardiomyocyte dysfunction.NPJ Regenerative medicine · 2024Article
- Spa2 remodels ADP-actin via molecular condensation under glucose starvation.Nature communications · 2024Article
- Article
- Multi-Omics Profiling of Hypertrophic Cardiomyopathy Reveals Altered Mechanisms in Mitochondrial Dynamics and Excitation-Contraction Coupling.International journal of molecular sciences · 2023Article
- Structural and functional analysis of actin point mutations leading to nemaline myopathy to elucidate their role in actin function.Biophysical reviews · 2022Article
- 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
- Article
- Dysregulation of lipid metabolism and appearance of slow myofiber-specific isoforms accompany the development of Wooden Breast myopathy in modern broiler chickens.Scientific reports · 2019Article
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- Actin dynamics in host-pathogen interaction.FEBS letters · 2018Review
- 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
- The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Archives of biochemistry and biophysics · 2017Article
- Crystal Structure of Leiomodin 2 in Complex with Actin: A Structural and Functional Reexamination.Biophysical journal · 2017Article
- A Third Look at the Structure of Leiomodin Bound to Actin.Biophysical journal · 2017Article
- Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 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
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Leiomodin (Lmod) is a class of potent tandem-G-actin-binding nucleators in muscle cells. Lmod mutations, deletion, or instability are linked to lethal nemaline myopathy. However, the lack of high-resolution structures of Lmod nucleators in action severely hampered our understanding of their essential cellular functions. Here we report the crystal structure of the actin-Lmod2162-495 nucleus. The structure contains two actin subunits connected by one Lmod2162-495 molecule in a non-filament-like conformation. Complementary functional studies suggest that the binding of Lmod2 stimulates ATP hydrolysis and accelerates actin nucleation and polymerization. The high level of conservation among Lmod proteins in sequence and functions suggests that the mechanistic insights of human Lmod2 uncovered here may aid in a molecular understanding of other Lmod proteins. Furthermore, our structural and mechanistic studies unraveled a previously unrecognized level of regulation in mammalian signal transduction mediated by certain tandem-G-actin-binding nucleators.
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