A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation

• Published in: PLoS biology Vol. 19; no. 12; p. e3001474
• Main Authors: Smith, Christopher E, Tsai, Yien Che, Liang, Yu-He, Khago, Domarin, Mariano, Jennifer, Li, Jess, Tarasov, Sergey G, Gergel, Emma, Tsai, Borong, Villaneuva, Matthew, Clapp, Michelle E, Magidson, Valentin, Chari, Raj, Byrd, R Andrew, Ji, Xinhua, Weissman, Allan M
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 08.12.2021; Public Library of Science (PLoS)
• Subjects: Amino Acid Sequence - genetics; Amino acids; Binding; Binding sites; Biology and Life Sciences; Bridges; Cell Line, Tumor; CRISPR; Degradation; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Endoplasmic Reticulum-Associated Degradation - genetics; Endoplasmic Reticulum-Associated Degradation - physiology; Experiments; Homeostasis; Humans; Hydrogen bonding; Hydrogen bonds; Hydrophobicity; Lipids; Mammals; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membrane Proteins - physiology; Membrane Proteins - ultrastructure; Membranes; Mutagenesis; Mutation; Physical Sciences; Plasmids; Protein Binding - genetics; Protein Domains - genetics; Proteins; Quality control; Research and Analysis Methods; Substrates; Ubiquitin; Ubiquitin-conjugating enzyme; Ubiquitin-Conjugating Enzymes - genetics; Ubiquitin-Conjugating Enzymes - metabolism; Ubiquitin-Conjugating Enzymes - physiology; Ubiquitin-Conjugating Enzymes - ultrastructure; Ubiquitin-protein ligase; Ubiquitination; Hong Kong China

Endoplasmic reticulum-associated degradation (ERAD) is a protein quality control pathway of fundamental importance to cellular homeostasis. Although multiple ERAD pathways exist for targeting topologically distinct substrates, all pathways require substrate ubiquitination. Here, we characterize a ke...