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CPEB2-eEF2 interaction impedes HIF-1alpha RNA translation.

Authors: Chen, PJ  Huang, YS 
Citation: Chen PJ and Huang YS, EMBO J. 2012 Feb 15;31(4):959-71. doi: 10.1038/emboj.2011.448. Epub 2011 Dec 9.
Pubmed: (View Article at PubMed) PMID:22157746
DOI: Full-text: DOI:10.1038/emboj.2011.448

Translation of mRNA into protein proceeds in three phases: initiation, elongation, and termination. Regulated translation allows the prompt production of selective proteins in response to physiological needs and is often controlled by sequence-specific RNA-binding proteins that function at initiation. Whether the elongation phase of translation can be modulated individually by trans-acting factors to synthesize polypeptides at variable rates remains to be determined. Here, we demonstrate that the RNA-binding protein, cytoplasmic polyadenylation element binding protein (CPEB)2, interacts with the elongation factor, eEF2, to reduce eEF2/ribosome-triggered GTP hydrolysis in vitro and slow down peptide elongation of CPEB2-bound RNA in vivo. The interaction of CPEB2 with eEF2 downregulates HIF-1alpha RNA translation under normoxic conditions; however, when cells encounter oxidative stress, CPEB2 dissociates from HIF-1alpha RNA, leading to rapid synthesis of HIF-1alpha for hypoxic adaptation. This study delineates the molecular mechanism of CPEB2-repressed translation and presents a unique model for controlling transcript-selective translation at elongation.

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CRRD Object Information
CRRD ID: 8553654
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.