Endoplasmic reticulum quality control (ERQC) pathways comprising chaperones, folding
enzymes, and degradation factors ensure the fidelity of ER protein folding and trafficking to …

Maintaining proteome integrity is essential for long-term viability of all organisms and is
overseen by intrinsic quality control mechanisms. The secretory pathway of eukaryotes …

Protein folding is inherently error prone, especially in the endoplasmic reticulum (ER). Even
with an elaborate network of molecular chaperones and protein folding facilitators …

ER-phagy (reticulophagy) defines the degradation of portions of the endoplasmic reticulum
(ER) within lysosomes or vacuoles. It is part of the self-digestion (ie, autophagic) programs …

The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where
nascent proteins encounter a specialized environment for their folding and maturation …

Significance: The endoplasmic reticulum (ER) is a specialized organelle for the folding and
trafficking of proteins, which is highly sensitive to changes in intracellular homeostasis and …

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 …

Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

The unfolded protein response (UPR) maintains endoplasmic reticulum (ER) proteostasis
through the activation of transcription factors such as XBP1s and ATF6. The functional …