| First Author | Chen PJ | Year | 2012 |
| Journal | EMBO J | Volume | 31 |
| Issue | 4 | Pages | 959-71 |
| PubMed ID | 22157746 | Mgi Jnum | J:181762 |
| Mgi Id | MGI:5314154 | Doi | 10.1038/emboj.2011.448 |
| Citation | Chen PJ, et al. (2012) CPEB2-eEF2 interaction impedes HIF-1alpha RNA translation. EMBO J 31(4):959-71 |
| abstractText | 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. |
