Additionally, our targeted pharmacological studies reveal that impaired force generation, mitochondrial dysfunction, and LD accumulation in LGMD2B are likely a secondary consequence to dysferlin‐deficiency‐induced Ca[2+] overload, while impaired membrane repair is directly caused by the lack of dysferlin.[9, 52] Finally, we also replicate some mouse preclinical drug responses, establishing human LGMD2B myobundles as a novel in vitro platform to promote the understanding and treatment of dysferlinopathy. The gene discussed is DYSF; the disease is neuromuscular disease caused by qualitative or quantitative defects of dysferlin.