Single-particle cryo-EM of APC/C-CDH1-UBE2C-Ubiquitin-CyclinB-NTD
Ontology highlight
ABSTRACT:
SUBMITTER: Tatyana Bodrug
PROVIDER: EMPIAR-11661 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Time-resolved cryo-EM (TR-EM) analysis of substrate polyubiquitination by the RING E3 anaphase-promoting complex/cyclosome (APC/C).
Bodrug Tatyana T Welsh Kaeli A KA Bolhuis Derek L DL Paulаkonis Ethan E Martinez-Chacin Raquel C RC Liu Bei B Pinkin Nicholas N Bonacci Thomas T Cui Liying L Xu Pengning P Roscow Olivia O Amann Sascha Josef SJ Grishkovskaya Irina I Emanuele Michael J MJ Harrison Joseph S JS Steimel Joshua P JP Hahn Klaus M KM Zhang Wei W Zhong Ellen D ED Haselbach David D Brown Nicholas G NG
Nature structural & molecular biology 20230921 11
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 el ...[more]
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