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Translation initiation mediated by nuclear cap-binding protein complex

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dc.contributor.authorRyu, Incheol-
dc.contributor.authorKim, Yoon Ki-
dc.date.accessioned2021-09-03T08:07:14Z-
dc.date.available2021-09-03T08:07:14Z-
dc.date.created2021-06-16-
dc.date.issued2017-04-
dc.identifier.issn1976-6696-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/84066-
dc.description.abstractIn mammals, cap-dependent translation of mRNAs is initiated by two distinct mechanisms: cap-binding complex (CBC; a heterodimer of CBP80 and 20)-dependent translation (CT) and eIF4E-dependent translation (ET). Both translation initiation mechanisms share common features in driving cap-dependent translation; nevertheless, they can be distinguished from each other based on their molecular features and biological roles. CT is largely associated with mRNA surveillance such as nonsense-mediated mRNA decay (NMD), whereas ET is predominantly involved in the bulk of protein synthesis. However, several recent studies have demonstrated that CT and ET have similar roles in protein synthesis and mRNA surveillance. In a subset of mRNAs, CT preferentially drives the cap-dependent translation, as ET does, and ET is responsible for mRNA surveillance, as CT does. In this review, we summarize and compare the molecular features of CT and ET with a focus on the emerging roles of CT in translation.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherKOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY-
dc.subjectMESSENGER-RNA DECAY-
dc.subjectEXON JUNCTION COMPLEX-
dc.subjectEUKARYOTIC TRANSLATION-
dc.subjectMAMMALIAN-CELLS-
dc.subjectHELICASE ACTIVITY-
dc.subjectGENE-EXPRESSION-
dc.subjectCBP80/20-DEPENDENT TRANSLATION-
dc.subjectPOLY(A)-BINDING PROTEIN-
dc.subjectUPF1 PHOSPHORYLATION-
dc.subjectMOLECULAR-MECHANISMS-
dc.titleTranslation initiation mediated by nuclear cap-binding protein complex-
dc.typeArticle-
dc.contributor.affiliatedAuthorKim, Yoon Ki-
dc.identifier.doi10.5483/BMBRep.2017.50.4.007-
dc.identifier.scopusid2-s2.0-85019001597-
dc.identifier.wosid000400527600007-
dc.identifier.bibliographicCitationBMB REPORTS, v.50, no.4, pp.186 - 193-
dc.relation.isPartOfBMB REPORTS-
dc.citation.titleBMB REPORTS-
dc.citation.volume50-
dc.citation.number4-
dc.citation.startPage186-
dc.citation.endPage193-
dc.type.rimsART-
dc.type.docTypeReview-
dc.identifier.kciidART002218047-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.subject.keywordPlusMESSENGER-RNA DECAY-
dc.subject.keywordPlusEXON JUNCTION COMPLEX-
dc.subject.keywordPlusEUKARYOTIC TRANSLATION-
dc.subject.keywordPlusMAMMALIAN-CELLS-
dc.subject.keywordPlusHELICASE ACTIVITY-
dc.subject.keywordPlusGENE-EXPRESSION-
dc.subject.keywordPlusCBP80/20-DEPENDENT TRANSLATION-
dc.subject.keywordPlusPOLY(A)-BINDING PROTEIN-
dc.subject.keywordPlusUPF1 PHOSPHORYLATION-
dc.subject.keywordPlusMOLECULAR-MECHANISMS-
dc.subject.keywordAuthorCBC-
dc.subject.keywordAuthoreIF4E-
dc.subject.keywordAuthorNMD-
dc.subject.keywordAuthorTranslation-
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