Leiomodin-3 (LMOD3)

Leiomodin-3 (LMOD3) is a muscle-specific actin nucleator that plays a central role in establishing and maintaining proper sarcomere structure in skeletal and cardiac muscles[1][4]. It localizes at the pointed ends of thin filaments, robustly catalyzing actin assembly to ensure correct filament elongation and spatial organization[1][4]. LMOD3 function is modulated by interaction with KLHL40 (which stabilizes LMOD3 by preventing ubiquitination and degradation), and is indispensable for sarcomere integrity—deficiency results in disorganized thin filaments and nemaline body formation[1][3][4]. Mutations, especially the G326R substitution in its leucine-rich repeat domain, abolish its actin-regulatory activity, causally linking LMOD3 deficiency to nemaline myopathy, marked by generalized muscle weakness and fast-fiber-specific atrophy[2][4][3]. LMOD3 is not currently a therapeutic target; it is instead a key structural regulator and genetic biomarker for specific congenital muscle disorders.

Other names

Leiomodin 3LMOD3Leiomodin, fetal formNEM10leiomodin 3 (fetal)leiomodin, fetal form