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 apoptosi...

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Published inAmerican Journal of Physiology: Cell Physiology Vol. 307; no. 7; pp. C582 - C594
Main Authors Dufey, Estefanie, Sepúlveda, Denisse, Rojas-Rivera, Diego, Hetz, Claudio
Format Journal Article
LanguageEnglish
Published United States American Physiological Society 01.10.2014
Subjects
Anatomy & physiology
Animals
Apoptosis
Disease
Endoplasmic Reticulum - metabolism
Endoplasmic Reticulum - pathology
Endoplasmic Reticulum Stress - genetics
Eukaryotes
Gene expression
Gene Expression Regulation
Humans
Metabolism
Protein folding
Proteins - genetics
Proteins - metabolism
Signal Transduction - genetics
Unfolded Protein Response - genetics
ER stress
UPR
protein misfolding
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Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Review-1
ISSN:0363-6143
1522-1563
DOI:10.1152/ajpcell.00258.2014