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Myomaker is a membrane activator of myoblast fusion and muscle formation

Author

Listed:
  • 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)

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.

Suggested Citation

  • Douglas P. Millay & Jason R. O’Rourke & Lillian B. Sutherland & Svetlana Bezprozvannaya & John M. Shelton & Rhonda Bassel-Duby & Eric N. Olson, 2013. "Myomaker is a membrane activator of myoblast fusion and muscle formation," Nature, Nature, vol. 499(7458), pages 301-305, July.
  • Handle: RePEc:nat:nature:v:499:y:2013:i:7458:d:10.1038_nature12343
    DOI: 10.1038/nature12343
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    Cited by:

    1. David Moi & Shunsuke Nishio & Xiaohui Li & Clari Valansi & Mauricio Langleib & Nicolas G. Brukman & Kateryna Flyak & Christophe Dessimoz & Daniele de Sanctis & Kathryn Tunyasuvunakool & John Jumper & , 2022. "Discovery of archaeal fusexins homologous to eukaryotic HAP2/GCS1 gamete fusion proteins," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Dandan Qian & Ye Cong & Runhao Wang & Quan Chen & Chuangye Yan & Deshun Gong, 2023. "Structural insight into the human SID1 transmembrane family member 2 reveals its lipid hydrolytic activity," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    3. Matthieu Dos Santos & Akansha M. Shah & Yichi Zhang & Svetlana Bezprozvannaya & Kenian Chen & Lin Xu & Weichun Lin & John R. McAnally & Rhonda Bassel-Duby & Ning Liu & Eric N. Olson, 2023. "Opposing gene regulatory programs governing myofiber development and maturation revealed at single nucleus resolution," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    4. Viviane Tran & Sarah Nahlé & Amélie Robert & Inès Desanlis & Ryan Killoran & Sophie Ehresmann & Marie-Pier Thibault & David Barford & Kodi S. Ravichandran & Martin Sauvageau & Matthew J. Smith & Marie, 2022. "Biasing the conformation of ELMO2 reveals that myoblast fusion can be exploited to improve muscle regeneration," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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