Spatiotemporal regulation of the GPCR activity of BAI3 by C1qL4 and Stabilin-2 controls myoblast fusion

Noumeira Hamoud, Viviane Tran, Takahiro Aimi, Wataru Kakegawa, Sylvie Lahaie, Marie-Pier Thibault, Ariane Pelletier, G. William Wong, In-San Kim, Artur Kania, Michisuke Yuzaki, Michel Bouvier and Jean-François Côté ()
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Noumeira Hamoud: Institut de Recherches Cliniques de Montréal (IRCM)
Viviane Tran: Institut de Recherches Cliniques de Montréal (IRCM)
Takahiro Aimi: Keio University School of Medicine
Wataru Kakegawa: Keio University School of Medicine
Sylvie Lahaie: Institut de Recherches Cliniques de Montréal (IRCM)
Marie-Pier Thibault: Institut de Recherches Cliniques de Montréal (IRCM)
Ariane Pelletier: Institut de Recherches Cliniques de Montréal (IRCM)
G. William Wong: Johns Hopkins University School of Medicine
In-San Kim: Korea Institute Science and Technology
Artur Kania: Institut de Recherches Cliniques de Montréal (IRCM)
Michisuke Yuzaki: Keio University School of Medicine
Michel Bouvier: Université de Montréal
Jean-François Côté: Institut de Recherches Cliniques de Montréal (IRCM)

Nature Communications, 2018, vol. 9, issue 1, 1-16

Abstract: Abstract Myoblast fusion is tightly regulated during development and regeneration of muscle fibers. BAI3 is a receptor that orchestrates myoblast fusion via Elmo/Dock1 signaling, but the mechanisms regulating its activity remain elusive. Here we report that mice lacking BAI3 display small muscle fibers and inefficient muscle regeneration after cardiotoxin-induced injury. We describe two proteins that repress or activate BAI3 in muscle progenitors. We find that the secreted C1q-like1–4 proteins repress fusion by specifically interacting with BAI3. Using a proteomic approach, we identify Stabilin-2 as a protein that interacts with BAI3 and stimulates its fusion promoting activity. We demonstrate that Stabilin-2 activates the GPCR activity of BAI3. The resulting activated heterotrimeric G-proteins contribute to the initial recruitment of Elmo proteins to the membrane, which are then stabilized on BAI3 through a direct interaction. Collectively, our results demonstrate that the activity of BAI3 is spatiotemporally regulated by C1qL4 and Stabilin-2 during myoblast fusion.

Date: 2018
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DOI: 10.1038/s41467-018-06897-5

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