DMD encodes dystrophin, a large structural protein that anchors the extracellular matrix to the cytoskeleton via F-actin and serves as a ligand for dystroglycan. Dystrophin is a key component of the dystrophin-associated glycoprotein complex, which accumulates at neuromuscular junctions and synapses throughout the peripheral and central nervous systems, providing structural stability to the sarcolemma and protecting muscle fibers from contraction-induced damage 1. The protein also participates in signaling events and synaptic transmission. Loss-of-function mutations in DMD cause Duchenne muscular dystrophy (DMD), a severe X-linked disorder affecting 1 in 5000 males, characterized by progressive muscle weakness, wheelchair dependence by age twelve, and death in the third decade due to respiratory and cardiac complications 1. Exonic deletions are the most common pathogenic variants, occurring in 90% of cases, with deletions in exons 45-55 representing 73% of all deletion patterns 2. Cardiac involvement is particularly significant, with higher frequencies of exons 45 and 46 involvement in DMD patients with cardiac dysfunction 3. Several FDA-approved therapies target DMD, including antisense oligonucleotides for exon skipping (eteplirsen, golodirsen, casimersen, viltolarsen) and gene therapy approaches (delandistrogene moxeparvovec) 45. Recent research highlights lysosomal dysfunction as a central pathophysiological mechanism that limits therapeutic efficacy, suggesting combination approaches pairing dystrophin restoration with lysosomal enhancement may provide synergistic benefits 6.