Abstract
The endoplasmic reticulum (ER) is an essential organelle for the eukaryotic cell. Beyond its involvement in the control of calcium and lipid homeostasis, it is also responsible for the folding, maturation, quality control, and traffic of secretory or transmembrane proteins. Nutrient deprivation, hypoxia, change in calcium homeostasis, or increased protein synthesis demand can provoke an accumulation of improperly folded proteins in this compartment, thereby causing ER stress and triggering the unfolded protein response (UPR). In human cells, the UPR relies on three ER stress sensors (IRE1α, PERK, and ATF6) and aims at restoring ER protein homeostasis (proteostasis) by attenuating global translation, increasing the transcription of specific genes (mostly encoding chaperones), foldases, or proteins of the ER-associated degradation (ERAD) machinery. If the UPR cannot restore ER proteostasis, it drives the cell into apoptosis. In this chapter, we present the UPR and its signaling pathways, with particular emphasis on gene expression reprogramming through epigenetic regulations, transcription factors, and chromatin changes, and we review their implications in human diseases.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
