One step at a time: endoplasmic reticulum-associated degradation

By S. Vembar, Jeffrey L. Brodsky. Nature reviews. Molecular cell biology, 2008

1,321 citations recorded by the source corpus.

Protein folding in the endoplasmic reticulum (ER) is monitored by ER quality control (ERQC) mechanisms. Proteins that pass ERQC criteria traffic to their final destinations through the secretory pathway, whereas non-native and unassembled subunits of multimeric proteins are degraded by the ER-associated degradation (ERAD) pathway. During ERAD, molecular chaperones and associated factors recognize and target substrates for retrotranslocation to the cytoplasm, where they are degraded by the ubiquitin–proteasome machinery. The discovery of diseases that are associated with ERAD substrates highlights the importance of this pathway. Here, we summarize our current understanding of each step during ERAD, with emphasis on the factors that catalyse distinct activities.

Subfields: Cell Biology, Epidemiology, Physiology

View Paper: https://www.semanticscholar.org/paper/7e84bc79e6cf09efb00191c903c6f1b3e82f8bda

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Citations in the corpus

• hERG K(+) channels: structure, function, and clinical significance. (2012, background): “At least 12 KCNH2 mutations that are predicted PKA Nucleus PIP2 IP3 +DAG SGK3 Synthesis Trafficking Degradation Endocytosis KCNQ1 KCNQ1 KCR1 hERG AT1 M3 AR45 Dihydrotestosterone Nedd4-2 PKG Low K+ Ceramide Cholesterol Progesterone Chronic stimulation Polyubiquitination Ubiquitination ERK1/2 Endoplas”
• Metformin promotes antitumor immunity via endoplasmic reticulum-associated degradation of PD-L1 (2018, neutral): “Metformin treatment induced the binding of endogenous PD-L1 to the ERAD components, SEL1L, HRD1, ERLEC1, and OS9 (Figure 4E, lines 2 vs 3).”