A role for actin flexibility in thin filament-mediated contractile regulation and myopathy

• Published in: Nature communications Vol. 11; no. 1; p. 2417
• Main Authors: Viswanathan, Meera C., Schmidt, William, Franz, Peter, Rynkiewicz, Michael J., Newhard, Christopher S., Madan, Aditi, Lehman, William, Swank, Douglas M., Preller, Matthias, Cammarato, Anthony
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 15.05.2020; Nature Publishing Group; Nature Portfolio
• Subjects: 119/118; 14; 14/19; 631/114; 631/443; 631/45; 631/57; 631/80; 64; 64/24; Actin; Actin Cytoskeleton - metabolism; Actins - chemistry; Actomyosin; Animals; Animals, Genetically Modified; Calcium-binding protein; Cardiac muscle; Cardiomyopathy; Cardiomyopathy, Hypertrophic; Computational Biology; Conformation; Drosophila melanogaster - metabolism; Female; Filaments; Flexibility; Flight, Animal; Humanities and Social Sciences; Humans; Hydrogen Bonding; In vivo methods and tests; Male; Microscopy, Fluorescence; Molecular Dynamics Simulation; multidisciplinary; Muscle Contraction; Muscles; Muscular Diseases - pathology; Muscular function; Mutation; Myopathy; Principal Component Analysis; Properties (attributes); Protein Multimerization; Residues; Science; Science (multidisciplinary); Skeletal muscle; Static Electricity; Transgenes; Translocation; Tropomyosin; Tropomyosin - chemistry; Troponin

Striated muscle contraction is regulated by the translocation of troponin-tropomyosin strands over the thin filament surface. Relaxation relies partly on highly-favorable, conformation-dependent electrostatic contacts between actin and tropomyosin, which position tropomyosin such that it impedes act...