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The Trithorax protein Ash1L promotes myoblast fusion by activating Cdon expression

Author

Listed:
  • Ilaria Castiglioni

    (IRCCS San Raffaele Scientific Institute)

  • Roberta Caccia

    (IRCCS San Raffaele Scientific Institute)

  • Jose Manuel Garcia-Manteiga

    (IRCCS San Raffaele Scientific Institute)

  • Giulia Ferri

    (IRCCS San Raffaele Scientific Institute)

  • Giuseppina Caretti

    (University of Milan)

  • Ivan Molineris

    (IRCCS San Raffaele Scientific Institute)

  • Kenichi Nishioka

    (Saga University
    RIKEN IMS)

  • Davide Gabellini

    (IRCCS San Raffaele Scientific Institute)

Abstract

Myoblast fusion (MF) is required for muscle growth and repair, and its alteration contributes to muscle diseases. The mechanisms governing this process are incompletely understood, and no epigenetic regulator has been previously described. Ash1L is an epigenetic activator belonging to the Trithorax group of proteins and is involved in FSHD muscular dystrophy, autism and cancer. Its physiological role in skeletal muscle is unknown. Here we report that Ash1L expression is positively correlated with MF and reduced in Duchenne muscular dystrophy. In vivo, ex vivo and in vitro experiments support a selective and evolutionary conserved requirement for Ash1L in MF. RNA- and ChIP-sequencing indicate that Ash1L is required to counteract Polycomb repressive activity to allow activation of selected myogenesis genes, in particular the key MF gene Cdon. Our results promote Ash1L as an important epigenetic regulator of MF and suggest that its activity could be targeted to improve cell therapy for muscle diseases.

Suggested Citation

  • Ilaria Castiglioni & Roberta Caccia & Jose Manuel Garcia-Manteiga & Giulia Ferri & Giuseppina Caretti & Ivan Molineris & Kenichi Nishioka & Davide Gabellini, 2018. "The Trithorax protein Ash1L promotes myoblast fusion by activating Cdon expression," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07313-8
    DOI: 10.1038/s41467-018-07313-8
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