Tampering with springs: phosphorylation of titin affecting the mechanical function of cardiomyocytes.

ABSTRACT: Reversible post-translational modifications of various cardiac proteins regulate the mechanical properties of the cardiomyocytes and thus modulate the contractile performance of the heart. The giant protein titin forms a continuous filament network in the sarcomeres of striated muscle cells, where it determines passive tension development and modulates active contraction. These mechanical properties of titin are altered through post-translational modifications, particularly phosphorylation. Titin contains hundreds of potential phosphorylation sites, the functional relevance of which is only beginning to emerge. Here, we provide a state-of-the-art summary of the phosphorylation sites in titin, with a particular focus on the elastic titin spring segment. We discuss how phosphorylation at spe

SUBMITTER: Hamdani N 

PROVIDER: S-EPMC5498327 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature