NDLI: An Upstream Open Reading Frame Regulates Translation of GADD34 during Cellular Stresses That Induce eIF2α $Phosphorylation^{*S⃞}$

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An Upstream Open Reading Frame Regulates Translation of GADD34 during Cellular Stresses That Induce eIF2α $Phosphorylation^{*S⃞}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lee, Yun-young Cevallos, Randal C. Jan, Eric
Description	Author Affiliation: Lee YY ( Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.)
Abstract	Cellular stress such as endoplasmic reticulum stress, hypoxia, and viral infection activates an integrated stress response, which includes the phosphorylation of the eukaryotic initiation factor 2α (eIF2α) to inhibit overall protein synthesis. Paradoxically, this leads to translation of a subset of mRNAs, like transcription factor ATF4, which in turn induces transcription of downstream stress-induced genes such as growth arrest DNA-inducible gene 34 (GADD34). GADD34 interacts with protein phosphatase 1 to dephosphorylate eIF2α, resulting in a negative feedback loop to recover protein synthesis and allow translation of stress-induced transcripts. Here, we show that GADD34 is not only transcriptionally induced but also translationally regulated to ensure maximal expression during eIF2α phosphorylation. GADD34 mRNAs are preferentially associated with polysomes during eIF2α phosphorylation, which is mediated by its 5′-untranslated region (5′UTR). The human GADD34 5′UTR contains two non-overlapping upstream open reading frames (uORFs), whereas the mouse version contains two overlapping and out of frame uORFs. Using 5′UTR GADD34 reporter constructs, we show that the downstream uORF mediates repression of basal translation and directs translation during eIF2α phosphorylation. Furthermore, we show that the upstream uORF is poorly translated and that a proportion of scanning ribosomes bypasses the upstream uORF to recognize the downstream uORF. These findings suggest that GADD34 translation is regulated by a unique 5′UTR uORF mechanism to ensure proper GADD34 expression during eIF2α phosphorylation. This mechanism may serve as a model for understanding how other 5′UTR uORF-containing mRNAs are regulated during cellular stress.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	11
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-03-13
Publisher Place	United States
Access Restriction	Open
Subject Keyword	5' Untranslated Regions Physiology Antigens, Differentiation Biosynthesis Cell Cycle Proteins Eukaryotic Initiation Factor-2 Metabolism Open Reading Frames Protein Biosynthesis Stress, Physiological Animals Genetics Cell Line, Tumor Mice Phosphorylation Polyribosomes Protein Phosphatase 1 RNA, Messenger Species Specificity Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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