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


ABSTRACT: 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-1? RNA translation under normoxic conditions; however, when cells encounter oxidative stress, CPEB2 dissociates from HIF-1? RNA, leading to rapid synthesis of HIF-1? 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.

SUBMITTER: Chen PJ 

PROVIDER: S-EPMC3280548 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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

Chen Po-Jen PJ   Huang Yi-Shuian YS  

The EMBO journal 20111209 4


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 th  ...[more]

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2024-09-24 | GSE242882 | GEO