| Literature DB >> 34985706 |
Hidetaka Katow1, Deepika Vasudevan1, Hyung Don Ryoo2.
Abstract
Wildtype or mutant proteins expressed beyond the capacity of a cell's protein folding system could be detrimental to general cellular function and survival. In response to misfolded protein overload in the endoplasmic reticulum (ER), eukaryotic cells activate the Unfolded Protein Response (UPR) that helps cells restore protein homeostasis in the endoplasmic reticulum (ER). As part of the UPR, cells attenuate general mRNA translation and activate transcription factors that induce stress-responsive gene expression.UPR signaling draws research interest in part because conditions that cause chronic protein misfolding in the ER or those that impair UPR signaling underlie several diseases including neurodegeneration, diabetes, and cancers. Model organisms are frequently employed in the field as the UPR pathways are generally well-conserved throughout phyla. Here, we introduce experimental procedures to detect UPR in Drosophila melanogaster.Entities:
Keywords: ATF4 (crc); Drosophila melanogaster; ER stress; Eye discs; Fat body; IRE1; PERK; Unfolded Protein Response; Xbp1
Mesh:
Year: 2022 PMID: 34985706 DOI: 10.1007/978-1-0716-1732-8_17
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745