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2003:
Harding Heather P; Zhang Yuhong; Zeng Huiquing; Novoa Isabel; Lu Phoebe D; Calfon Marcella; Sadri Navid; Yun Chi; Popko Brian; Paules Richard; Stojdl David F; Bell John C; Hettmann Thore; Leiden Jeffrey M; Ron David
An integrated stress response regulates amino acid metabolism and resistance to oxidative stress.
Molecular cell 2003;
11(
3):.
Eukaryotic cells respond to unfolded proteins in their endoplasmic reticulum (ER stress), amino acid starvation, or oxidants by phosphorylating the alpha subunit of translation initiation factor 2 (eIF2alpha). This adaptation inhibits general protein synthesis while promoting translation and expression of the transcription factor ATF4. Atf4(-/-) cells are impaired in expressing genes involved in amino acid import, glutathione biosynthesis, and resistance to oxidative stress. Perk(-/-) cells, lacking an upstream ER stress-activated eIF2alpha kinase that activates Atf4, accumulate endogenous peroxides during ER stress, whereas interference with the ER oxidase ERO1 abrogates such accumulation. A signaling pathway initiated by eIF2alpha phosphorylation protects cells against metabolic consequences of ER oxidation by promoting the linked processes of amino acid sufficiency and resistance to oxidative stress.
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