Tatyana Bodrug, Kaeli A Welsh, Derek L Bolhuis, Ethan Paulаkonis, Raquel C Martinez-Chacin, Bei Liu, Nicholas Pinkin, Thomas Bonacci, Liying Cui, Pengning Xu, Olivia Roscow, Sascha Josef Amann, Irina Grishkovskaya, Michael J Emanuele, Joseph S Harrison, Joshua P Steimel, Klaus M Hahn, Wei Zhang, Ellen D Zhong, David Haselbach, Nicholas G Brown
Substrate polyubiquitination drives a myriad of cellular processes, including the cell cycle, apoptosis and immune responses. Polyubiquitination is highly dynamic, and obtaining mechanistic insight has thus far required artificially trapped structures to stabilize specific steps along the enzymatic process. So far, how any ubiquitin ligase builds a proteasomal degradation signal, which is canonically regarded as four or more ubiquitins, remains unclear. Here we present time-resolved cryogenic electron microscopy studies of the 1...
September 21, 2023: Nature Structural & Molecular Biology