Quality control: ER-associated degradation: protein quality control and beyond.

By Annamaria Ruggiano, O. Foresti, Pedro Carvalho. Journal of Cell Biology, 2014

602 citations recorded by the source corpus.

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 these potentially toxic species are detected and eliminated. The best characterized of these pathways, the ER-associated protein degradation (ERAD), monitors the folding of membrane and secretory proteins whose biogenesis takes place in the endoplasmic reticulum (ER). There is also increasing evidence that ERAD controls other ER-related functions through regulated degradation of certain folded ER proteins, further highlighting the role of ERAD in cellular homeostasis.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d76c50b976943384f2504e589b798c1778a67074

Citations in the corpus

• Elements of the ERAD ubiquitin ligase Doa10 regulating sequential poly-ubiquitylation of its targets (2022, unknown): “Maintaining protein homeostasis at the ER is therefore crucial, and eukaryotes have developed multiple quality control mechanisms to prevent the accumulation of misfolded proteins in the ER (Babour et al., 2010; Braakman and Hebert, 2013; Ruggiano et al., 2014; Satpute-Krishnan et al., 2014; Szoradi”