Abstract: Intracellular protein degradation is an essential process for all living forms to survive. All eukaryotic organisms majorly utilize Ubiquitin-Proteasome system (UPS) to degrade damaged, non-functional & retired proteins; and thereby maintain protein homeostasis to carry out their cellular processes. In general, proteins are degraded in the cells when tagged by another small protein (of MW 8 KDa) – “Ubiquitin” and brought to a huge degradation machine – “26S proteasome”. 26S proteasome is a multi-subunit protein complex (of MW ~2500 KDa), that proteolyzes the target proteins into peptides and releases the ubiquitin tag. But, at times of emergency or under certain cellular stress when 26S proteasomes turn non-functional, cells rely on a smaller machine – “20S proteasome” (of MW ~700 KDa), which degrades proteins in a ubiquitin-independent manner. We recently discovered that under oxidative stress and human heart failure 20S proteasome becomes the major protease and alleviates the hypoxia-induced proteotoxicity for survival. During this emergency, surprisingly the tagged ubiquitins are degraded as collateral damage.

Meeting ID: 978 0448 4199
Passcode: 649442