Proteostasis control by the unfolded protein response

By C. Hetz, É. Chevet, Scott A Oakes. Nature Cell Biology, 2015

714 citations recorded by the source corpus.

Stress induced by accumulation of misfolded proteins in the endoplasmic reticulum is observed in many physiological and pathological conditions. To cope with endoplasmic reticulum stress, cells activate the unfolded protein response, a dynamic signalling network that orchestrates the recovery of homeostasis or triggers apoptosis, depending on the level of damage. Here we provide an overview of recent insights into the mechanisms that cells employ to maintain proteostasis and how the unfolded protein response determines cell fate under endoplasmic reticulum stress.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/0681765666e2cca29e4f198991c38345c2800de8

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. É. Chevet
2. C. Hetz
3. F. Papa

In Epidemiology

1. C. Hetz
2. É. Chevet
3. F. Papa

In Surgery

1. É. Chevet
2. C. Hetz
3. F. Papa

Citations in the corpus

• The Unfolded Protein Response and Cell Fate Control. (2017, neutral): “The function of ATF6 is also regulated by phosphorylation, proteasome-mediated degradation, glycosylation, and reduction of luminal cysteines (Hetz et al., 2015).”
• Endoplasmic reticulum stress signalling and the pathogenesis of non-alcoholic fatty liver disease. (2018, background): “If the adaptive UPR is overwhelmed by chronic or acute ER stress, it may become unable to preserve ER function, switching to a “terminal UPR” that induces cell death(48) through pathways involving ROS production, upregulation of pro-apoptotic BCL-2 family members, microRNA regulation, sustained ER-c”