Dystrophin-glycoprotein complex (DGC) connects the F-Actin cytoskeleton on the inner surface of muscle fibers to the surrounding extracellular matrix, through the cell membrane interface. A deficiency in this protein contributes to Duchenne (DMD) and Becker (BMD) muscular dystrophies. The human dystrophin gene measures 2.4 megabases, has more than 80 exons, produces a 14 kb mRNA and contains at least eight independent tissue-specific promoters and two poly A sites. The dystrophin mRNA can undergo differential splicing and produce a range of transcripts that encode a large set of proteins. Dystrophin represents approximately 0.002% of total striated muscle protein and localizes to triadic junctions in skeletal muscle, where it is thought to influence calcium ion homeostasis and force transmission.

1. Baradaran-Heravi A et al. Novel small molecules potentiate premature termination codon readthrough by aminoglycosides. Nucleic Acids Res 44:6583-98 (2016).
2. Karolczak J et al. Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei. Histochem Cell Biol 139:873-85 (2013).