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Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
DC Field | Value | Language |
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dc.contributor.author | Kim, V. Narry | - |
dc.contributor.author | Kataoka, Naoyuki | - |
dc.contributor.author | Dreyfuss, Gideon | - |
dc.date.accessioned | 2021-01-31T08:12:42Z | - |
dc.date.available | 2021-01-31T08:12:42Z | - |
dc.date.created | 2020-07-16 | - |
dc.date.issued | 2001-09 | - |
dc.identifier.citation | Science, Vol.293 No.5536, pp.1832-1836 | - |
dc.identifier.issn | 0036-8075 | - |
dc.identifier.other | 107108 | - |
dc.identifier.uri | https://hdl.handle.net/10371/171903 | - |
dc.description.abstract | Nonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically (similar to 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm. | - |
dc.language | 영어 | - |
dc.publisher | American Association for the Advancement of Science | - |
dc.title | Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex | - |
dc.type | Article | - |
dc.contributor.AlternativeAuthor | 김빛내리 | - |
dc.identifier.doi | 10.1126/science.1062829 | - |
dc.citation.journaltitle | Science | - |
dc.identifier.wosid | 000170894400048 | - |
dc.identifier.scopusid | 2-s2.0-0035823150 | - |
dc.citation.endpage | 1836 | - |
dc.citation.number | 5536 | - |
dc.citation.startpage | 1832 | - |
dc.citation.volume | 293 | - |
dc.identifier.sci | 000170894400048 | - |
dc.description.isOpenAccess | N | - |
dc.contributor.affiliatedAuthor | Kim, V. Narry | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | PRE-MESSENGER-RNA | - |
dc.subject.keywordPlus | TRANSLATIONAL TERMINATION CODON | - |
dc.subject.keywordPlus | OPEN READING FRAME | - |
dc.subject.keywordPlus | NUCLEAR EXPORT | - |
dc.subject.keywordPlus | BINDING-PROTEINS | - |
dc.subject.keywordPlus | HNRNP PROTEINS | - |
dc.subject.keywordPlus | K-PROTEIN | - |
dc.subject.keywordPlus | SURVEILLANCE | - |
dc.subject.keywordPlus | YEAST | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
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