Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere.

This has been shown in recent studies where biomechanical properties of the sarcolemma and its links through costameres to the contractile apparatus were measured,[11] and helps to prevent muscle fiber injury.

Movement of thin filaments (actin) creates a pulling force on the extracellular connective tissue that eventually becomes the tendon of the muscle.

[12] Dystrophin deficiency has been definitively established as one of the root causes of the general class of myopathies collectively referred to as muscular dystrophy.

The deletions of one or several exons of the dystrophin DMD gene cause Duchenne and Becker muscular dystrophies.

The theory currently most commonly used to predict whether a variant will result in a DMD or BMD phenotype, is the reading frame rule.

[23] Clinically relevant pathology can be observed at 8 weeks after birth, with continued gradual deterioration of muscle function.

Dystrophin has been shown to interact with: A variant of the DMD gene, which is on the X chromosome, named B006, appears to be an introgression from a Neanderthal-modern human mating.