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Sumoylation of eIF4E activates mRNA translation
Author(s) -
Xu Xiang,
Vatsyayan Jaya,
Gao Chenxi,
Bakkenist Christopher J,
Hu Jing
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.18
Subject(s) - eif4e , sumo protein , translation (biology) , microbiology and biotechnology , messenger rna , eukaryotic initiation factor , eukaryotic translation , protein biosynthesis , biology , initiation factor , eukaryotic translation initiation factor 4 gamma , eif4a1 , eif4ebp1 , ubiquitin , biochemistry , gene
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.