Dystrophin is a large (~400 kDa) structural protein encoded by the DMD gene on the X chrX 1. It anchors the extracellular matrix to the cytoskeleton via F-actin binding and functions as a ligand for dystroglycan, serving as a core component of the dystrophin-associated glycoprotein complex at the sarcolemma and neuromuscular junction [UniProt]. Dystrophin maintains muscle fiber integrity and protects against contraction-induced damage by stabilizing the sarcolemma 2. Mutations in DMD cause Duchenne muscular dystrophy (DMD), an X-linked disease affecting 1 in 3500-5000 males, characterized by progressive muscle weakness, wheelchair dependence by age twelve, and death in the third decade from respiratory and cardiac complications 23. Exonic deletions and duplications are the primary pathogenic variants, with deletions in exons 45-55 accounting for 73% of deletion patterns 4. The milder allelic form, Becker muscular dystrophy, results from in-frame mutations producing partially functional dystrophin 5. Dystrophin deficiency compromises muscle fiber stability and function, eventually causing muscle degeneration 2. Multiple therapeutic approaches target dystrophin restoration, including exon-skipping, stop codon read-through, AAV-mediated gene therapy, and genome editing strategies 563. Recent evidence demonstrates that transcriptional adaptation upregulates utrophin, the dystrophin paralogue, in response to DMD mutations, suggesting additional compensatory mechanisms 7.