期刊
EMBO REPORTS
卷 11, 期 4, 页码 299-304出版社
WILEY
DOI: 10.1038/embor.2010.18
关键词
eIF4E; mRNA translation; oncogenic transformation; sumoylation; translation initiation
资金
- National Institutes of Health [CA128681]
- Pittsburgh Foundation
- Direct For Biological Sciences [1021767] Funding Source: National Science Foundation
- NATIONAL CANCER INSTITUTE [R21CA128681] Funding Source: NIH RePORTER
Eukaryotic translation initiation factor 4E (eIF4E) is the cap-binding protein that binds the 5' cap structure of cellular messenger RNAs (mRNAs). Despite the obligatory role of eIF4E in cap-dependent mRNA translation, how the translation activity of eIF4E is controlled remains largely undefined. Here, we report that mammalian eIF4E is regulated by SUMO1 (small ubiquitin-related modifier 1) conjugation. eIF4E sumoylation promotes the formation of the active eIF4F translation initiation complex and induces the translation of a subset of proteins that are essential for cell proliferation and preventing apoptosis. Furthermore, disruption of eIF4E sumoylation inhibits eIF4E-dependent protein translation and abrogates the oncogenic and antiapoptotic functions associated with eIF4E. These data indicate that sumoylation is a new fundamental regulatory mechanism of protein synthesis. Our findings suggest further that eIF4E sumoylation might be important in promoting human cancers.
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