DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Kyoung Mi | ko |
dc.contributor.author | Cho, Hana | ko |
dc.contributor.author | Choi, Kobong | ko |
dc.contributor.author | Kim, Jaedong | ko |
dc.contributor.author | Kim, Bong-Woo | ko |
dc.contributor.author | Ko, Young-Gyu | ko |
dc.contributor.author | Jang, Sung Key | ko |
dc.contributor.author | Kim, Yoon Ki | ko |
dc.date.accessioned | 2022-08-04T07:00:58Z | - |
dc.date.available | 2022-08-04T07:00:58Z | - |
dc.date.created | 2022-08-04 | - |
dc.date.created | 2022-08-04 | - |
dc.date.issued | 2009-09 | - |
dc.identifier.citation | GENES & DEVELOPMENT, v.23, no.17, pp.2033 - 2045 | - |
dc.identifier.issn | 0890-9369 | - |
dc.identifier.uri | http://hdl.handle.net/10203/297806 | - |
dc.description.abstract | During or right after mRNA export via the nuclear pore complex (NPC) in mammalian cells, mRNAs undergo translation mediated by nuclear cap-binding proteins 80 and 20 (CBP80/20). After CBP80/20-dependent translation, CBP80/20 is replaced by cytoplasmic cap-binding protein eIF4E, which directs steady-state translation. Nonsense-mediated mRNA decay (NMD), one of the best-characterized mRNA surveillance mechanisms, has been shown to occur on CBP80/20-bound mRNAs. However, despite the tight link between CBP80/20-dependent translation and NMD, the underlying molecular mechanism and cellular factors that mediate CBP80/20-dependent translation remain obscure. Here, we identify a new MIF4G domain-containing protein, CTIF (CBP80/20-dependent translation initiation factor). CTIF interacts directly with CBP80 and is part of the CBP80/20-dependent translation initiation complex. Depletion of endogenous CTIF from an in vitro translation system selectively blocks the translation of CBP80-bound mRNAs, while addition of purified CTIF restores it. Accordingly, down-regulation of endogenous CTIF abrogates NMD. Confocal microscopy shows that CTIF is localized to the perinuclear region. Our observations demonstrate the existence of CBP80/20-dependent translation and support the idea that CBP80/20-dependent translation is mechanistically different from steady-state translation through identification of a specific cellular protein, CTIF. | - |
dc.language | English | - |
dc.publisher | COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT | - |
dc.title | A new MIF4G domain-containing protein, CTIF, directs nuclear cap-binding protein CBP80/20-dependent translation | - |
dc.type | Article | - |
dc.identifier.wosid | 000269482300006 | - |
dc.identifier.scopusid | 2-s2.0-69749116302 | - |
dc.type.rims | ART | - |
dc.citation.volume | 23 | - |
dc.citation.issue | 17 | - |
dc.citation.beginningpage | 2033 | - |
dc.citation.endingpage | 2045 | - |
dc.citation.publicationname | GENES & DEVELOPMENT | - |
dc.identifier.doi | 10.1101/gad.1823409 | - |
dc.contributor.localauthor | Kim, Yoon Ki | - |
dc.contributor.nonIdAuthor | Kim, Kyoung Mi | - |
dc.contributor.nonIdAuthor | Cho, Hana | - |
dc.contributor.nonIdAuthor | Choi, Kobong | - |
dc.contributor.nonIdAuthor | Kim, Jaedong | - |
dc.contributor.nonIdAuthor | Kim, Bong-Woo | - |
dc.contributor.nonIdAuthor | Ko, Young-Gyu | - |
dc.contributor.nonIdAuthor | Jang, Sung Key | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | CTIF | - |
dc.subject.keywordAuthor | nonsense-mediated mRNA decay | - |
dc.subject.keywordAuthor | nuclear cap-binding protein CBP80/20 | - |
dc.subject.keywordAuthor | eukaryotic translation initiation factor 4G | - |
dc.subject.keywordAuthor | steady-state translation | - |
dc.subject.keywordPlus | MESSENGER-RNA DECAY | - |
dc.subject.keywordPlus | NONSENSE-MEDIATED DECAY | - |
dc.subject.keywordPlus | EXON JUNCTION COMPLEX | - |
dc.subject.keywordPlus | MAMMALIAN-CELLS | - |
dc.subject.keywordPlus | POLY(A)-BINDING PROTEIN | - |
dc.subject.keywordPlus | QUALITY-CONTROL | - |
dc.subject.keywordPlus | SURVEILLANCE | - |
dc.subject.keywordPlus | INITIATION | - |
dc.subject.keywordPlus | UPF1 | - |
dc.subject.keywordPlus | TRANSCRIPTS | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.