Myomaker is a membrane activator of myoblast fusion and muscle formation

Douglas P. Millay, Jason R. O’Rourke, Lillian B. Sutherland, Svetlana Bezprozvannaya, John M. Shelton, Rhonda Bassel-Duby and Eric N. Olson ()
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Douglas P. Millay: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
Jason R. O’Rourke: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
Lillian B. Sutherland: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
Svetlana Bezprozvannaya: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
John M. Shelton: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
Rhonda Bassel-Duby: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA
Eric N. Olson: University of Texas Southwestern Medical Center, Dallas, Texas 75390, USA

Nature, 2013, vol. 499, issue 7458, 301-305

Abstract: Abstract 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.

Date: 2013
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DOI: 10.1038/nature12343

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