The N-terminal region of myopalladin binds to the nuclear protein CARP, known to regulate gene expression in muscle.

[10] Myopalladin has dual subcellular localization, residing in both the nucleus and sarcomere/I-bands in muscle.

Accordingly, myopalladin has functions in both sarcomere assembly and in control of gene expression.

[5] Specifics of these functions were gleaned from studies involving MYPN mutants associated with various cardiomyopathies.

The Q529X myopalladin mutant demonstrated incompetence in recruiting key binding partners such as desmin, alpha-actinin and CARP to the Z-disc during myofibrilogenesis.