Correction: SUMO-2 Promotes mRNA Translation by Enhancing Interaction between eIF4E and eIF4G
نویسندگان
چکیده
The 11,12, and 13 authors are listed out of order. The correct order is: Li-zhao Chen , Xiang-yun Li , Hong Huang , Wei Xing , Wei Guo , Jing He , Zhi-ya Sun , Anxiong Luo , Hua-ping Liang , Jing Hu , Zheng-guo Wang , Yun-sheng Xu , Xiang Xu 1,3,* First department, State Key Laboratory of Trauma, Burn and Combined Injury, Research Institute of Surgery and Daping Hospital, Third Military Medical University, Chongqing, China Department of Neurosurgery, Research Institute of Surgery and Daping Hospital, Third Military Medical University, Chongqing, China Cell-based Biotherapy Center, Research Institute of Surgery and Daping Hospital, Third Military Medical University, Chongqing, China Fourth department, State Key Laboratory of Trauma, Burn and Combined Injury, Research Institute of Surgery and Daping Hospital, Third Military Medical University, Chongqing, China Department of Pharmacology and Chemical Biology, University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA. Department of Dermatology, First Affiliated Hospital of Wenzhou Medical College, Wenzhou Zhejiang, China #These authors contributed equally to this work. *These authors are co-corresponding authors
منابع مشابه
SUMO-2 Promotes mRNA Translation by Enhancing Interaction between eIF4E and eIF4G
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 transla...
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In eukaryotes, mRNA translation is dependent on the cap-binding protein eIF4E. Through its simultaneous interaction with the mRNA cap structure and with the ribosome-associated eIF4G adaptor protein, eIF4E physically posits the ribosome at the 5' extremity of capped mRNA. eIF4E activity is regulated by phosphorylation on a unique site by the eIF4G-associated kinase MNK. eIF4E assembly with the ...
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The eukaryotic mRNA 3' poly(A) tail and the 5' cap cooperate to synergistically enhance translation. This interaction is mediated by the cap-binding protein eIF4E, the poly(A) binding protein (PABP), and eIF4G, a scaffolding protein that bridges between eIF4E and PABP to bring about the circularization of the mRNA. The translational repressor, Paip2 (PABP-interacting protein 2), inhibits transl...
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