Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated …
J Hwang, L Qi - Trends in biochemical sciences, 2018 - cell.com
Endoplasmic reticulum (ER)-associated degradation (ERAD) and the unfolded protein response (UPR) are two key quality-control machineries in the cell. ERAD is responsible for …
Z Sun, JL Brodsky - Journal of Cell Biology, 2019 - rupress.org
Protein folding is inherently error prone, especially in the endoplasmic reticulum (ER). Even with an elaborate network of molecular chaperones and protein folding facilitators …
N Zheng, N Shabek - Annual review of biochemistry, 2017 - annualreviews.org
Ubiquitin E3 ligases control every aspect of eukaryotic biology by promoting protein ubiquitination and degradation. At the end of a three-enzyme cascade, ubiquitin ligases …
JC Christianson, P Carvalho - The EMBO journal, 2022 - embopress.org
The endoplasmic reticulum (ER) is a large, dynamic, and multifunctional organelle. ER protein homeostasis is essential for the coordination of its diverse functions and depends on …
X Wu, TA Rapoport - Current opinion in cell biology, 2018 - Elsevier
Misfolded proteins of the endoplasmic reticulum (ER) are discarded by a conserved process, called ER-associated protein degradation (ERAD). ERAD substrates are retro-translocated …
INTRODUCTION Protein homeostasis in the endoplasmic reticulum (ER) is maintained by a quality control system. When a newly synthesized ER protein misfolds, it is ultimately …
Summary The Cdc48 ATPase and its cofactors Ufd1/Npl4 (UN) extract polyubiquitinated proteins from membranes or macromolecular complexes, but how they perform these …
JT Marinko, H Huang, WD Penn, JA Capra… - Chemical …, 2019 - ACS Publications
Advances over the past 25 years have revealed much about how the structural properties of membranes and associated proteins are linked to the thermodynamics and kinetics of …