[8] Myotilin was originally identified as a novel alpha-actinin binding partner with two Ig-like domains, that localized to the Z-disc.

[10] By contrast, the N-terminal part of myotilin is unique, consisting of a serine-rich region with no homology to known proteins.

A ternary complex myotilin/actin/alpha-actinin can be observed in vitro and actin bundles formed under these conditions appear more tightly packed than those induced by alpha-actinin alone.

Targeted disruption of the myotilin gene in mice does not cause significant alterations in muscle function.

It has been shown that actin binding properties of myotilin housing pathogenic mutations (Ser55Phe, Thr57Ile, Ser60Cys, and Ser95Ile) are normal,[18] albeit with a slower rate of degradation.