Measuring ER stress and the unfolded protein response using mammalian tissue culture system

By C. M. Oslowski, F. Urano. Methods in Enzymology, 2011

874 citations recorded by the source corpus.

The endoplasmic reticulum (ER) functions to properly fold and process secreted and transmembrane proteins. Environmental and genetic factors that disrupt ER function cause an accumulation of misfolded and unfolded proteins in the ER lumen, a condition termed ER stress. ER stress activates a signaling network called the Unfolded Protein Response (UPR) to alleviate this stress and restore ER homeostasis, promoting cell survival and adaptation. However, under unresolvable ER stress conditions, the UPR promotes apoptosis. Here we discuss the current methods to measure ER stress levels, UPR activation, and subsequent pathways in mammalian cells. These methods will assist us in understanding the UPR and its contribution to ER stress related-disorders such as diabetes and neurodegeneration.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/3529fc78eb78966191acd873dbab5b8830345fea

Citations in the corpus

• A multiplexed single-cell CRISPR screening platform enables systematic dissection of the unfolded protein response (2016, neutral): “…ACTB (oBA74: GCTACGAGCTGCCTGACG, oBA75: GGCTGGAAGAGTGCCTCA), CHOP (oBA249: AGAACCAGGAAACGGAAACAGA, oBA250: TCTCCTTCATGCGCTGCTTT) (Oslowski and Urano, 2011), SEC61A1 (oBA360: TGCAAAGCAGCTGAAGGA, oBA361: ATGCACAGCCCACCAAAG), SSR2 (oBA364: TTCACCTCGGCAACAATTACT, oBA365:…”