Symposium — Monday, April 24, 2017 — 8:00 AM - 10:00 AM — , Room W192B
Cardiovascular Section — Chair: Noah Weisleder — Co-Chair: Xuejun Wang
The ubiquitin proteasome system (UPS) is a principal pathway for degradation of proteins in most cell types and is considered to be an important mechanism for the regulation for numerous cellular processes. Post-translational modifications by ubiquitin (ubiquitination) or ubiquitin-like proteins such as SUMO (SUMOylation), NEDD8 (neddylation), etc. are shown to regulate not only the degradation of the modified proteins via the UPS and autophagy but also the function/activities of the modified proteins. While these systems are essential in many cell types an increasing body of evidence indicates that this system is particularly important in heart resident cells. Protein turnover must function properly to maintain normal physiologic function of a number of different cellular functions in cardiomyocytes and other cardiac resident cell types, including ion channel function, vesicle trafficking, Ca2+ handling and regulation of contractile filaments. Alteration of ubiquitin proteasome activity contributes to progression of multiple cardiovascular diseases, including thrombosis, response to myocardial infarction, arrhythmias and congestive heart failure. Recent studies have begun to determine the specific proteasomal degradation mechanisms underlying cardiovascular disease have been identified. Other studies show that these pathways are clinically relevance. Many specific E3 ligases have been shown to be involved the physiology and pathophysiology of the heart and this session will detail some of these excited findings and link the ubiquitin proteasome system to several different aspects of cardiac function and dysfunction. In parallel, neddylation and SUMOylation have recently been shown to regulate cardiac function via modifying specific cardiac proteins, promising exciting translational potentials to provide novel therapies for cardiovascular disease.