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The mammalian unfolded protein response.
In the endoplasmic reticulum (ER), secretory and transmembrane proteins fold into their native conformation and undergo posttranslational modifications important for their activity and structure.Expand
Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
It is proposed that mRNA released from disassembled polysomes is sorted and remodeled at SGs, from which selected transcripts are delivered to PBs for degradation, an interaction that is promoted by the related mRNA decay factors TTP and BRF1. Expand
A trip to the ER: coping with stress.
This review highlights advances in how the unfolded protein response is regulated and how its effects radiate beyond the immediate realm of protein secretion and attempts to forecast important issues that must be addressed soon. Expand
ER stress and the unfolded protein response.
A model in which the activity of UPR signaling pathways reflects the biosynthetic activity of the ER is proposed, which shows that this information is integrated into control of cellular events, which were previously not considered to be under control of ER signaling pathways. Expand
From endoplasmic-reticulum stress to the inflammatory response
New observations suggest that the unfolded-protein response can initiate inflammation, and the coupling of these responses in specialized cells and tissues is now thought to be fundamental in the pathogenesis of inflammatory diseases. Expand
ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
It is shown that eIF2α-phosphorylation-attenuated protein synthesis, and not Atf4 mRNA translation, promotes cell survival, and suggesting that limiting protein synthesis will be therapeutic for diseases caused by protein misfolding in the ER. Expand
Translational control is required for the unfolded protein response and in vivo glucose homeostasis.
It is demonstrated that regulation of translation through eIF2alpha phosphorylation is essential for the ER stress response and in vivo glucose homeostasis. Expand
IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response.
It is proposed that nuclear- localized IRE1alpha and cytoplasmic-localized ATF6 signaling pathways merge through regulation of XBP1 activity to induce downstream gene expression. Expand
The endoplasmic reticulum and the unfolded protein response.
The endoplasmic reticulum is the site where proteins enter the secretory pathway, and those processes that prevent accumulation of unfolded proteins in the ER lumen are highly regulated by an intracellular signaling pathway known as the unfolded protein response (UPR). Expand
Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival
The data demonstrate that Nrf2 is a critical effector of PERK-mediated cell survival, and it is demonstrated that cells harboring a targeted deletion of NRF2 exhibit increased cell death relative to wild-type counterparts following exposure to ER stress. Expand