Myosin binding protein-C (MyBP-C) consists of fast skeletal (fMyBP-C), slow skeletal (sMyBP-C), and cardiac isoforms (cMyBP-C). Both cMyBP-C and sMyBP-C have been demonstrated to be necessary for normal striated muscle function, and they are important regulators of actin-myosin interactions. However, the precise function of fMyBP-C is unknown, and its role in skeletal muscle remains enigmatic. Thus, this project will characterize the regulatory roles of sMyBP-C in skeletal muscle in health and disease. Despite their names, fast and slow isoforms of MyBP-C are not exclusively expressed in fast-twitch or slow-twitch skeletal muscles. Rather, they are coexpressed in varying ratios, and each may have distinct functions. Therefore, understanding how sMyBP-C regulates muscle contraction at the cellular and molecular level is particularly important in the context of muscle disease, which is often characterized by muscle weakness and impaired function.

References :

• » Lin B, Govindan S, Lee K, Ji X, Zhao P, Han R, Runte K.E, Craig R, Palmer B.M and Sadayappan S. Cardiac myosin binding protein-C plays no regulatory role in skeletal muscle structure and function. PLoS ONE 8(7): e69671.