Kelch-like protein 41 (KLHL41)

Kelch-like protein 41 (KLHL41) is a muscle-specific, structural protein crucial for the assembly, organization, and maintenance of sarcomeres in skeletal muscle. It acts primarily as a molecular chaperone, preventing aggregation and promoting the stability of the large sarcomeric protein nebulin. KLHL41 achieves this function through poly-ubiquitination-dependent mechanisms distinct from most Kelch family proteins, which more commonly target proteins for degradation. Loss-of-function mutations in KLHL41 cause nemaline myopathy, a severe congenital disorder characterized by abnormal muscle structure, sarcomere disorganization, and early-onset muscle weakness or perinatal lethality[1][2][3][4][5][6]. KLHL41 also interacts with other sarcomeric proteins, including NRAP and filamin-C, but its stabilizing effect is predominantly on nebulin. It is not currently considered a direct therapeutic target, drug receptor, or enzyme.

Other names

Kelch-like protein 41KLHL41KBTBD10KRP1SarcosinKel-like protein 23Kelch repeat and BTB domain-containing protein 10Kelch-related protein 1sarcomeric muscle protein