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dc.contributor.author최준호-
dc.date.accessioned2019-07-17T01:42:33Z-
dc.date.available2019-07-17T01:42:33Z-
dc.date.issued2019-02-
dc.identifier.citationCELL REPORTS, v. 26, NO 8, Page. 2126-2126en_US
dc.identifier.issn2211-1247-
dc.identifier.urihttps://www.sciencedirect.com/science/article/pii/S221112471930138X?via%3Dihub-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/107487-
dc.description.abstractExon junction complexes (EJCs) loaded onto spliced mRNAs during splicing serve as molecular markers for various post-transcriptional gene-regulatory processes, including nonsense-mediated mRNA decay (NMD). Although the composition and structure of EJCs are well characterized, the mechanism regulating EJC deposition remains unknown. Here we find that threonine 163 (T163) within the RNA-binding motif of eIF4A3 (a core EJC component) is phosphorylated by cyclin-dependent protein kinases 1 and 2 in a cell cycle-dependentmanner. T163 phosphorylation hinders binding of eIF4A3 to spliced mRNAs and other EJC components. Instead, it promotes association of eIF4A3 with CWC22, which guides eIF4A3 to an active spliceosome. These molecular events ensure the fidelity of specific deposition of the EJC similar to 20-24 nt up-stream of an exon-exon junction. Accordingly, NMD is affected by T163 phosphorylation. Collectively, our data provide evidence that T163 phosphorylation affects EJC formation and, consequently, NMD efficiency in a cell cycle-dependent manner.en_US
dc.description.sponsorshipWe thank Niels Gehring for providing plasmid pCZ-CWC22 and Melisa Moore for pCN-MS2-Y14 and pCN-MS2-MAGOH. This work was supported by a National Research Foundation (NRF) of Korea grant funded by the Korean government (Ministry of Science, ICT, and Future Planning; NRF-2015R1A3A2033665 and NRF-2018R1A5A1024261), by a Korea University future research grant (K1720051), and by a Korea University grant, South Korea. I.R. and Y.S.W. were supported in part by the NRF funded by the Ministry of Education, Science and Technology, South Korea (NRF-2016R1D1A1B03933894 and NRF-2016R1A6A3A11933515, respectively).en_US
dc.language.isoenen_US
dc.publisherCELL PRESSen_US
dc.subjectEXON JUNCTION COMPLEXen_US
dc.subjectMESSENGER-RNA DECAYen_US
dc.subjectENHANCES TRANSLATIONen_US
dc.subjectCRYSTAL-STRUCTUREen_US
dc.subjectMAMMALIAN-CELLSen_US
dc.subjectPROTEINen_US
dc.subjectREVEALSen_US
dc.subjectIDENTIFICATIONen_US
dc.subjectCOREen_US
dc.subjectSEQen_US
dc.titleeIF4A3 Phosphorylation by CDKs Affects NMD during the Cell Cycleen_US
dc.typeArticleen_US
dc.relation.no8-
dc.relation.volume26-
dc.identifier.doi10.1016/j.celrep.2019.01.101-
dc.relation.page2126-2126-
dc.relation.journalCELL REPORTS-
dc.contributor.googleauthorRyu, Incheol-
dc.contributor.googleauthorWon, You-Sub-
dc.contributor.googleauthorHa, Hongseok-
dc.contributor.googleauthorKim, Eunjin-
dc.contributor.googleauthorPark, Yeonkyoung-
dc.contributor.googleauthorKim, Min Kyung-
dc.contributor.googleauthorKwon, Do Hoon-
dc.contributor.googleauthorChoe, Junho-
dc.contributor.googleauthorSong, Hyun Kyu-
dc.contributor.googleauthorJung, Hosung-
dc.relation.code2019036884-
dc.sector.campusS-
dc.sector.daehakCOLLEGE OF NATURAL SCIENCES[S]-
dc.sector.departmentDEPARTMENT OF LIFE SCIENCE-
dc.identifier.pidjcho2711-
dc.identifier.researcherIDE-3410-2019-
dc.identifier.orcidhttp://orcid.org/0000-0002-2365-3755-


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