Speaker: Dr. Tang Xiaomeng, University Medical Center Göttingen (UMG)
Date and time: May 28, 16:00–17:00
Venue: Auditorium, Y Building
Host: Wolfgang Baumeister
Abstract:
The proteasome, a multi-subunit proteolytic machine, plays a crucial role in cellular homeostasis by eliminating misassembled, dysfunctional, and surplus proteins. Previous studies have revealed that proteasomes can aggregate into storage granules (PSGs) when glucose is depleted. However, despite biochemical exploration, the enigmatic structure of PSGs remains elusive. In our research, we employ state-of-the-art Cryo-electron tomography (Cryo-ET) to uncover the in situ structure of PSGs. Our findings reveal that proteasome 26S trimers are stored in a paracrystalline arrangement. Additionally, we depict the PSG formation process, transitioning from a proliferating state to a quiescent state.
I will introduce the Cryo-ET workflow and highlight several new optional techniques. Additionally, I will discuss strategies for faster data collection in transmission electron microscopy (TEM).
Biography:
2022-2024, Postdoc Research Fellow; University Medical Center Göttingen, Göttingen, Germany
2019-2022, Postdoc Research Fellow; Max-Planck-Institute of Biochemistry, Martinsried, Germany
2017-2019, Visiting Scholar; iHmuan Institute, ShanghaiTech University, Shanghai, China
2012-2017, Ph.D., Biological Chemistry and Molecular Biology, Institute of Biophysics, Chinese Academy of Sciences, China