Septins, including Septin7, are GTP-binding proteins that form the cytoskeleton's fourth component. While their importance in various cell types is known, Septin7's role in skeletal muscle remains unclear. In a study using C2C12 myogenic cells, researchers explored the effects of forchlorfenuron (FCF) on cell proliferation, filament formation, and migration. FCF reduced cell proliferation, caused structural changes in Septin7 filaments, and decreased cell migration, with Septin7 knockdown cultures showing less impact. These findings highlight Septin7's critical involvement in skeletal muscle migration, proliferation, and dynamics, with potential implications for muscle-related pathologies like neurodegenerative diseases and muscle dystrophies.