Hamoud, Noumeira Tran, Viviane Aimi, Takahiro Kakegawa, Wataru Lahaie, Sylvie Thibault, Marie-Pier Pelletier, Ariane Wong, G. William Kim, In-San Kania, Artur Yuzaki, Michisuke Bouvier, Michel Cote, Jean-Francois 2024-01-19T21:34:22Z 2024-01-19T21:34:22Z 2021-09-04 2018-10 2041-1723 https://pubs.kist.re.kr/handle/201004/120870 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. English Nature Publishing Group Spatiotemporal regulation of the GPCR activity of BAI3 by C1qL4 and Stabilin-2 controls myoblast fusion Article 10.1038/s41467-018-06897-5 1 Nature Communications, v.9 Nature Communications 9 Y scie scopus 000448414100020 2-s2.0-85055614656 Multidisciplinary Sciences Science & Technology - Other Topics Article CELL CORPSE CLEARANCE COUPLED RECEPTOR BAI3 MYOGENIC DIFFERENTIATION MUSCLE DEVELOPMENT G-PROTEIN IN-VIVO ANGIOGENESIS INHIBITOR-1 C1Q-LIKE PROTEINS APOPTOTIC CELLS SKELETAL-MUSCLE