Mutations in tropomyosin genes TPM1 and TPM3 alter actin-myosin interactions and thin filament dynamics, leading to various types of cardiomyopathy and skeletal muscle diseases.
-dependent manner. It also participates in the maintenance of thin filament length by regulation of tropomodulin and leiomodin, the pointed end-binding proteins. Because the size of the overlap between actin and myosin filaments affects the number of myosin heads which interact with actin, the filament length is one of the determinants of force development. Numerous point mutations in genes encoding tropomyosin lead to single amino acid substitutions along the entire length of the coiled coil that are associated with various types of cardiomyopathy and skeletal muscle disease. Specific regions of tropomyosin interact with different binding partners; therefore, the mutations affect diverse tropomyosin functions. In this review, results of studies on mutations in the genes TPM1 and TPM3, encoding Tpm1.1 and Tpm3.12, are described. The paper is particularly focused on mutation-dependent alterations in the mechanisms of actin-myosin interactions and dynamics of the thin filament at the pointed end.
Joanna Moraczewska (Wed,) conducted a review in Cardiomyopathy and congenital myopathy. Mutations in TPM1 and TPM3 genes was evaluated. Mutations in tropomyosin genes TPM1 and TPM3 alter actin-myosin interactions and thin filament dynamics, leading to various types of cardiomyopathy and skeletal muscle diseases.