The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles

• Published in: International journal of molecular sciences Vol. 23; no. 10; p. 5306
• Main Authors: Szikora, Szilárd, Görög, Péter, Mihály, József
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 10.05.2022; MDPI
• Subjects: Actin; Actin Cytoskeleton; Actins - physiology; Calcium-binding protein; Cardiomyopathy; Dilated cardiomyopathy; Elongation; Filaments; Humans; Insects; Lattices; length regulation; Microscopy; Muscle Contraction; Muscles; Muscular function; Mutation; Myopathy; Myosin; Nemaline myopathy; Physiology; Proteins; Regulation; Review; sarcomere; Sarcomeres; thin filament; Tropomyosin; Tropomyosin - genetics; Troponin; actin; thin filament; myopathy; length regulation; sarcomere
• ISSN: 1422-0067; 1661-6596; 1422-0067
• DOI: 10.3390/ijms23105306

The actin containing tropomyosin and troponin decorated thin filaments form one of the crucial components of the contractile apparatus in muscles. The thin filaments are organized into densely packed lattices interdigitated with myosin-based thick filaments. The crossbridge interactions between these myofilaments drive muscle contraction, and the degree of myofilament overlap is a key factor of contractile force determination. As such, the optimal length of the thin filaments is critical for efficient activity, therefore, this parameter is precisely controlled according to the workload of a given muscle. Thin filament length is thought to be regulated by two major, but only partially understood mechanisms: it is set by (i) factors that mediate the assembly of filaments from monomers and catalyze their elongation, and (ii) by factors that specify their length and uniformity. Mutations affecting these factors can alter the length of thin filaments, and in human cases, many of them are linked to debilitating diseases such as nemaline myopathy and dilated cardiomyopathy.