Endoplasmic reticulum stress response in yeast and humans. Issue 4 (1st July 2014)

• Record Type: Journal Article
• Authors: Wu, Haoxi; Ng, Benjamin S. H.; Thibault, Guillaume
• Is Part Of: Bioscience reports. Volume 34:Issue 4(2014)
• Publication Date: 2014-07-01
• Subjects: ER stress -- IRE1 -- lipid disequilibrium -- protein homoeostasis -- unfolded protein response -- UPR-related diseases. The UPR (unfolded protein response) is activated to alleviate the effects of ER (endoplasmic reticulum) stress and is highly conserved from yeast to human. In this review -- we summarize the major advances in yeast and humans; Molecular biology -- Periodicals; Cytology -- Periodicals; 572.8
• DOI: 10.1042/BSR20140058
• Languages: English
• ISSNs: 0144-8463

Abstract

Abstract : Stress pathways monitor intracellular systems and deploy a range of regulatory mechanisms in response to stress. One of the best-characterized pathways, the UPR (unfolded protein response), is an intracellular signal transduction pathway that monitors ER (endoplasmic reticulum) homoeostasis. Its activation is required to alleviate the effects of ER stress and is highly conserved from yeast to human. Although metazoans have three UPR outputs, yeast cells rely exclusively on the Ire1 (inositol-requiring enzyme-1) pathway, which is conserved in all Eukaryotes. In general, the UPR program activates hundreds of genes to alleviate ER stress but it can lead to apoptosis if the system fails to restore homoeostasis. In this review, we summarize the major advances in understanding the response to ER stress in Sc ( Saccharomyces cerevisiae ), Sp ( Schizosaccharomyces pombe ) and humans. The contribution of solved protein structures to a better understanding of the UPR pathway is discussed. Finally, we cover the interplay of ER stress in the development of diseases.