Post-translational regulation of cardiac myosin binding protein-C: A graphical review

• Published in: Cellular signalling Vol. 76; p. 109788
• Main Authors: Main, Alice, Fuller, William, Baillie, George S.
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.12.2020
• Subjects: Animals; Cardiac contractility; Cardiac myosin binding protein C; Carrier Proteins - physiology; Heart Failure - metabolism; Humans; Myocardium - cytology; Myocardium - metabolism; Myocardium - pathology; Posttranslational modification; Protein Binding; Protein Processing, Post-Translational; Sarcomeres - metabolism; Posttranslational modification; Cardiac contractility; Cardiac myosin binding protein C
• ISSN: 0898-6568; 1873-3913; 1873-3913
• DOI: 10.1016/j.cellsig.2020.109788

Cardiac myosin binding protein-C (cMyBP-C) is a fundamental component of the cardiac sarcomere involved in regulating systolic and diastolic activity, processes which must be tightly maintained to preserve cardiac function. Importantly, as a non-enzymatic protein, cMyBP-C relies solely on post-translational modifications and protein-protein interactions in order to modulate its function, and does so through phosphorylation, glutathionylation and acetylation amongst others. Although some are better understood than others, these modifications may represent novel therapeutic routes to modulate cMyBP-C function in the treatment of cardiac disease. •Cardiac myosin binding protein-C (cMyBP-C) is a vital component of the sarcomere that regulates cardiac contractility.•Our understanding of cMyBP-C’s relationship with myosin, actin and other sarcomeric proteins continues to evolve.•CMyBP-C is subject to several important post-translational modifications that regulate its function in health and disease.•We discuss the advances in understanding these post-translational modifications, along with the challenges to overcome.