CHE 598 Seminar: Thick-Filament, Regulatory Protein Interactions In The Cardiac Sarcomere
About the event
SPEAKER: Dr. Bertrand Tanner, Associate Professor, College of Veterinary Medicine, WSU
BIOGRAPHY:
Dr. Tanner’s laboratory studies cardiac and skeletal muscle biology underlying physiological function and pathophysiological dysfunction. With a focus on mechanical and biochemical mechanisms that enable the myosin motor protein network to coordinate contractility over the molecular, cellular, and tissue levels, thereby powering blood flow and locomotion. Dr. Tanner’s background in physics, bioengineering, computational biology, and biomechanics all come together to tackle difficult and interesting questions about normal and diseased muscle function from a multi-disciplinary perspective. He loves mentoring and training students who are interested in multi-scale and multi-disciplinary research studies to understand how biological systems work. Muscles have an amazing variety of functions, and Dr. Tanner is hopeful that defining how different components of the system operate as a whole will ultimately guide innovative approaches to ameliorate dysfunctional contraction with disease.
ABSTRACT:
The heart comprises several proteins that work together to properly facilitate force production and pump blood throughout the body. Cardiac myosin binding protein-C (cMyBP-C) is a thick-filament protein, and mutations in cMyBP-C are frequently linked with clinical cases heart disease called hypertrophic cardiomyopathy. Myosin regulatory light chain (RLC) is another thick-filament protein; RLC is a subunit of myosin located within the myosin neck region that modulates contractile dynamics via its phosphorylation state. Previous biochemistry studies have suggested that cMyBP-C and RLC may interact with each other within the cardiac sarcomere, although structural characteristics of the muscle cell are lost with solution biochemistry assays. Thus, little is known about the effects of these potential cMyBP-C and RLC interactions on muscle force production and cardiac contractility. I will present some recently published work and some new, preliminary data that suggests cMyBP-C and RLC may act in concert to regulate contractility in healthy hearts. Mutations to these proteins that lead to HCM (or a loss of phosphorylation with disease progression) may disrupt important interactions between these thick-filament regulatory proteins.