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 …

Even with the assistance of many cellular factors, a significant fraction of newly synthesized
proteins ends up misfolded. Cells evolved protein quality control systems to ensure that …

Membrane-bound and soluble proteins of the secretory pathway are commonly glycosylated
in the endoplasmic reticulum. These adducts have many biological functions, including …

Endoplasmic reticulum (ER)-associated protein degradation (ERAD) eliminates misfolded or
unassembled proteins from the ER. ERAD targets are selected by a quality control system …

Misfolded proteins of the ER are retrotranslocated to the cytosol, where they are
polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To …

The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER
quality control (ERQC) system. The ERQC facilitates folding and modification of secretory …

Many misfolded endoplasmic reticulum (ER) proteins are eliminated by ERAD, a process in
which substrates are polyubiquitylated and moved into the cytosol for proteasomal …

After insertion into the endoplasmic reticulum (ER), proteins that fail to fold there are
destroyed. Through a process termed dislocation such misfolded proteins arrive in the …

DnaJ is a molecular chaperone and the prototypical member of the J‐protein family. J
proteins are defined by the presence of a J domain that can regulate the activity of 70‐kDa …

Misfolded, luminal endoplasmic reticulum (ER) proteins are retrotranslocated into the cytosol
and degraded by the ubiquitin/proteasome system. This ERAD-L pathway requires a protein …