Skeletal myosin binding protein-C isoforms regulate thin filament activity in a Ca²⁺-dependent manner.

ABSTRACT: Muscle contraction, which is initiated by Ca²⁺, results in precise sliding of myosin-based thick and actin-based thin filament contractile proteins. The interactions between myosin and actin are finely tuned by three isoforms of myosin binding protein-C (MyBP-C): slow-skeletal, fast-skeletal, and cardiac (ssMyBP-C, fsMyBP-C and cMyBP-C, respectively), each with distinct N-terminal regulatory regions. The skeletal MyBP-C isoforms are conditionally coexpressed in cardiac muscle, but little is known about their function. Therefore, to characterize the functional differences and regulatory mechanisms among these three isoforms, we expressed recombinant N-terminal fragments and examined their effect on contractile properties in biophysical assays. Addition of the fragments to in vitr

SUBMITTER: Lin BL 

PROVIDER: S-EPMC5805719 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature