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SUMO-2 promotes mRNA translation by enhancing interaction between eIF4E and eIF4G

Chen, LZ and Li, XY and Huang, H and Xing, W and Guo, W and He, J and Sun, ZY and Luo, AX and Liang, HP and Hu, J and Xu, X and Xu, YS and Wang, ZG (2014) SUMO-2 promotes mRNA translation by enhancing interaction between eIF4E and eIF4G. PLoS ONE, 9 (6).

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Small ubiquitin-like modifier (SUMO) proteins regulate many important eukaryotic cellular processes through reversible covalent conjugation to target proteins. In addition to its many well-known biological consequences, like subcellular translocation of protein, subnuclear structure formation, and modulation of transcriptional activity, we show here that SUMO-2 also plays a role in mRNA translation. SUMO-2 promoted formation of the active eukaryotic initiation factor 4F (eIF4F) complex by enhancing interaction between Eukaryotic Initiation Factor 4E (eIF4E) and Eukaryotic Initiation Factor 4G (eIF4G), and induced translation of a subset of proteins, such as cyclinD1 and c-myc, which essential for cell proliferation and apoptosis. As expected, overexpression of SUMO-2 can partially cancel out the disrupting effect of 4EGI-1, a small molecule inhibitor of eIF4E/eIF4G interaction, on formation of the eIF4F complex, translation of the cap-dependent protein, cell proliferation and apoptosis. On the other hand, SUMO-2 knockdown via shRNA partially impaired cap-dependent translation and cell proliferation and promoted apoptosis. These results collectively suggest that SUMO-2 conjugation plays a crucial regulatory role in protein synthesis. Thus, this report might contribute to the basic understanding of mammalian protein translation and sheds some new light on the role of SUMO in this process. © 2014 Chen et al.


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Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Chen, LZ
Li, XY
Huang, H
Xing, W
Guo, W
He, J
Sun, ZY
Luo, AX
Liang, HP
Hu, Jjih25@pitt.eduJIH25
Xu, X
Xu, YS
Wang, ZG
ContributionContributors NameEmailPitt UsernameORCID
Date: 27 June 2014
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 9
Number: 6
DOI or Unique Handle: 10.1371/journal.pone.0100457
Schools and Programs: School of Medicine > Pharmacology and Chemical Biology
Refereed: Yes
Date Deposited: 26 Sep 2014 14:31
Last Modified: 26 Jan 2019 10:55


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