ArticleNature structural & molecular biology2023
Cryo-EM structures of Myomaker reveal a molecular basis for myoblast fusion.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 7 citations in OpenAlex.
- Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4.Nature communications · 2026Article
- Article
- CHAMP1 is an essential regulator for human myoblast fusion and muscle development.Nature communications · 2026Article
- β-Nicotinamide Mononucleotide Inhibits Cellular Senescence in Mouse C2C12 Skeletal Muscle Cells.Journal of aging research · 2026Article
- Differentially expressed fusogens specify myocyte states to drive myogenesis.Development (Cambridge, England) · 2025Article
- Ectopic expression of Myomaker and Myomixer in slow muscle cells induces slow muscle fusion and myofiber death.Journal of genetics and genomics = Yi chuan xue bao · 2024Article
- MTM1-mediated production of phosphatidylinositol 5-phosphate fuels the formation of podosome-like protrusions regulating myoblast fusion.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular regulation of myocyte fusion.Current topics in developmental biology · 2024Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The fusion of mononucleated myoblasts produces multinucleated muscle fibers leading to the formation of skeletal muscle. Myomaker, a skeletal muscle-specific membrane protein, is essential for myoblast fusion. Here we report the cryo-EM structures of mouse Myomaker (mMymk) and Ciona robusta Myomaker (cMymk). Myomaker contains seven transmembrane helices (TMs) that adopt a G-protein-coupled receptor-like fold. TMs 2-4 form a dimeric interface, while TMs 3 and 5-7 create a lipid-binding site that holds the polar head of a phospholipid and allows the alkyl tails to insert into Myomaker. The similarity of cMymk and mMymk suggests a conserved Myomaker-mediated cell fusion mechanism across evolutionarily distant species. Functional analyses demonstrate the essentiality of the dimeric interface and the lipid-binding site for fusogenic activity, and heterologous cell-cell fusion assays show the importance of transcellular interactions of Myomaker protomers for myoblast fusion. Together, our findings provide structural and functional insights into the process of myoblast fusion.
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