Myopalladin (MYPN)

Myopalladin is a large (145 kDa) structural protein encoded by the MYPN gene and specifically expressed in striated muscle, where it is localized primarily to the sarcomeric Z-line and I-band[1][5]. It contains five immunoglobulin-like domains and a proline-rich region, enabling it to tether key muscle structural proteins: it links nebulin (skeletal muscle) or nebulette (heart) to alpha-actinin, contributing to the assembly and stability of the sarcomere[1][2][5]. Myopalladin has dual localization in the nucleus and sarcomere; in addition to its structural role, it interacts with nuclear proteins such as cardiac ankyrin repeat protein (CARP/ANKRD1), thus participating in mechanosensitive signaling and regulation of muscle gene expression[1][2][5]. MYPN mutations are linked to several myopathies and cardiomyopathies, including dilated, hypertrophic, and restrictive forms, as well as nemaline and cap myopathy[1][3][5]. Loss of function leads to disorganized sarcomere structure, impaired actin dynamics, and disruption of the serum response factor (SRF) signaling pathway required for normal muscle function[5][6]. Currently, myopalladin is not considered a direct therapeutic target; it has no known interacting drugs and is not classified as a receptor, enzyme, transporter, or classical signaling molecule[1][3][5]. However, MYPN gene variants serve as genetic biomarkers in the diagnosis of inherited cardiomyopathies and myopathies[1][3][5].

Other names

MYPNMYOP145 kDa sarcomeric proteinsarcomeric protein myopalladinCMD1DDCMH22CMYO24CMYP24NEM11RCM4