The 26S proteasome is the most complex ATP-dependent protease machinery, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated proteins and plays fundamentally indispensable roles in regulating almost all major aspects of cellular activities. To serve as the sole terminal “processor” for myriad ubiquitylation pathways, the proteasome evolved exceptional adaptability in dynamically organizing a large network of proteins, including ubiquitin receptors, shuttle factors, deubiquitinases, AAA-ATPase unfoldases, and ubiquitin ligases, to enable substrate selectivity and processing efficiency and to achieve regulation precision of a vast diversity of substrates. The inner working of the 26S proteasome is among the most sophisticated, enigmatic mechanisms of enzyme machinery in eukaryotic cells.
At this webinar, Dr Youdong Mao, Peking University / Dana-Farber Cancer Institute (part of Harvard Medical School), presents some of the work from his laboratory. With his students and fellow scientists, Dr Mao has pioneered the applications of deep learning in improving the cryo-EM data processing pipeline and determined numerous high resolution cryo-EM structures and conformational dynamics of human 26S proteasome and inflammasome under a variety of biochemical conditions. His work has substantially advanced our understanding of the inner working and autoregulation of the 26S proteasome, one of the most enigmatic holoenzyme machines generally found in cells.
For more information about the Biochemistry Focus webinar series, visit www.biochemistry.org/webinars
