Year: 2011
Type: review
Abstract: Myosin-binding protein C (MyBP-C) is a thick filament protein consisting of 1274 amino acid residues (149 kDa) that was identified by Starr and Offer over 30 years ago as a contaminant present in a preparation of purified myosin. Since then, numerous studies have defined the muscle-specific isoforms, the structure, and the importance of the proteins in normal striated muscle structure and function. Underlying the critical role the protein plays, it is now apparent that mutations in the cardiac isoform (cMyBP-C) are responsible for a substantial proportion (30-40%) of genotyped cases of familial hypertrophic cardiomyopathy. Although generally accepted that MyBP-C can interact with all three filament systems within the sarcomere (the thick, thin, and titin filaments), the exact nature of these interactions and the functional consequences of modified binding remain obscure. In addition to these structural considerations, cMyBP-C can serve as a point of convergence for signaling processes in the cardiomyocyte via post-translational modifications mediated by kinases that phosphorylate residues in the cardiac-specific isoform sequence. Thus, cMyBP-C is a critical nodal point that has both important structural and signaling roles and whose modifications are known to cause significant human cardiac disease.
Source: Journal of Biological Chemistry
Authors: Jeanne James, Jeffrey Robbins
Institution: Cincinnati Children's Hospital Medical Center
Language: English
Subfield: Cardiology and Cardiovascular Medicine
Field: Medicine
Domain: Health Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: G1106861790, G1531132452, Signaling Processes Underlying Cardiovascular Function, Cardiac Myosin Binding Protein-C: Structure, Function, and Regulation, G5581717129, Genetic and Molecular Signaling in Heart Failure, Cardiomyocyte Toxicity and Heart Failure in Desmin Related Cardiomyopathy, G9000102780
OpenAlex ID: W2051058132