The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Myomaker is a membrane activator of myoblast fusion and muscle formation
Open accessAbstract
Fusion of myoblasts is essential for the formation of multi-nucleated muscle fibres. However, the identity of muscle-specific proteins that directly govern this fusion process in mammals has remained elusive. Here we identify a muscle-specific membrane protein, named myomaker, that controls myoblast fusion. Myomaker is expressed on the cell surface of myoblasts during fusion and is downregulated thereafter. Overexpression of myomaker in myoblasts markedly enhances fusion, and genetic disruption of myomaker in mice causes perinatal death due to an absence of multi-nucleated muscle fibres. Remarkably, forced expression of myomaker in fibroblasts promotes fusion with myoblasts, demonstrating the direct participation of this protein in the fusion process. Pharmacological perturbation of the actin cytoskeleton abolishes the activity of myomaker, consistent with previous studies implicating actin dynamics in myoblast fusion. These findings reveal a long-sought myogenic fusion protein that controls mammalian myoblast fusion and provide new insights into the molecular underpinnings of muscle formation.
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Cites
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Self-citationBuilding Muscle: Molecular Regulation of Myogenesis
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Self-citationMyoD and the transcriptional control of myogenesis
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Metadata
- Authors
- Millay, D. P., O’Rourke, J. R., Sutherland, L. B., Bezprozvannaya, S., Shelton, J. M., Bassel-Duby, R., & Olson, E. N.
- Venue
- Nature
- Published
- 2013-07
- Volume
- 499
- Issue
- 7458
- Pages
- 301-305
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2009100350
- Cited by
- 577
- References
- 31
- FWCI
- 9.82
- Type
- journal article
- Language
- en
- Open access
- green
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- Millay, D. P., O’Rourke, J. R., Sutherland, L. B., Bezprozvannaya, S., Shelton, J. M., Bassel-Duby, R., & Olson, E. N. (2013). Myomaker is a membrane activator of myoblast fusion and muscle formation. Nature. https://doi.org/10.1038/nature12343
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