Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview.
Increased demand on the protein folding capacity of the endoplasmic reticulum (ER) engages an adaptive reaction known as the unfolded protein response (UPR). The UPR regulates protein translation and the expression of numerous target genes that contribute to restore ER homeostasis or induce apoptosis of irreversibly damaged cells. UPR signaling is highly regulated and dynamic and integrates information about the type, intensity, and duration of the stress stimuli, thereby determining cell fate. Recent advances highlight novel physiological outcomes of the UPR beyond specialized secretory cells, particularly in innate immunity, metabolism, and cell differentiation. Here we discuss studies on the fine-tuning of the UPR and its physiological role in diverse organs and diseases.
['Dufey|Estefanie|E|', 'Sepúlveda|Denisse|D|', 'Rojas-Rivera|Diego|D|', 'Hetz|Claudio|C|']
D000818:Animals D017209:Apoptosis D004194:Disease D004721:Endoplasmic Reticulum D059865:Endoplasmic Reticulum Stress D005786:Gene Expression Regulation D006801:Humans D011506:Proteins D015398:Signal Transduction D056811:Unfolded Protein Response
UPR ER stress protein misfolding