Lipid-mediated phase separation of AGO proteins on the ER controls nascent-peptide ubiquitination
Yajie Gao, Yuanxiang Zhu, Hailong Wang, Ying Cheng, Dongbo Zhao, Qinmiao Sun, Dahua Chen
Abstract
. The ER-localized AGO condensates recruit the E3 ubiquitin ligase Ltn1 to catalyze nascent-peptide ubiquitination and coordinate with the VCP-Ufd1-Npl4 complex to process unwanted protein products for proteasomal degradation. Collectively, our study provides insight into the understanding of post-transcription-translation coupling controlled by AGOs via lipid-mediated phase separation.
Topics & Concepts
BiologyEndoplasmic reticulumCell biologyUbiquitin ligaseUbiquitinEndoplasmic-reticulum-associated protein degradationUbiquitin-conjugating enzymeBiochemistryUnfolded protein responseGeneRNA Interference and Gene DeliveryEndoplasmic Reticulum Stress and DiseaseRNA Research and Splicing