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A new function of ROD1 in nonsense-mediated mRNA decay

dc.contributor.authorBrazão, Tiago França
dc.contributor.authorDemmers, J.
dc.contributor.authorvan IJcken, W.
dc.contributor.authorStrouboulis, J.
dc.contributor.authorFornerod, M.
dc.contributor.authorRomão, Luísa
dc.contributor.authorGrosveld, F.G.
dc.date.accessioned2012-07-04T15:04:32Z
dc.date.available2012-07-04T15:04:32Z
dc.date.issued2012-03-21
dc.description.abstractRNA-binding proteins play a crucial role in the post-transcriptional regulation of gene expression. Polypyrimidine tract binding protein (PTB in humans) has been extensively characterized as an important splicing factor, and has additional functions in 3' end processing and translation. ROD1 is a PTB paralog containing four RRM (RNA recognition motif) domains. Here, we discover a function of ROD1 in nonsense-mediated mRNA decay (NMD). We show that ROD1 and the core NMD factor UPF1 interact and co-regulate an extensive number of target genes. Using a reporter system, we demonstrate that ROD1, similarly to UPF1 and UPF2, is required for the destabilization of a known NMD substrate. Finally, we show through RIP-seq that ROD1 and UPF1 associate with a significant number of common transcripts.por
dc.identifier.citationFEBS Lett. 2012 Apr 24;586(8):1101-10. Epub 2012 Mar 21por
dc.identifier.issn014-5793
dc.identifier.otherdoi.org/10.1016/j.febslet.2012.03.015
dc.identifier.urihttp://hdl.handle.net/10400.18/875
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversionhttp://ac.els-cdn.com/99F2182F-294D-4EFC-8ADD-3E43FB18B5DB/FinalDownload/DownloadId-CA388036D3AE994DE22B17E2E652CDCD/99F2182F-294D-4EFC-8ADD-3E43FB18B5DB/S0014579312002025/1-s2.0-S0014579312002025-main.pdf?_tid=03033ad3280936bbee217fb38404abe4&acdnat=1341414077_fc59747c105616bebbdcef26b8a8c5a9por
dc.subjectDoenças Genéticaspor
dc.subjectGenómica Funcional e Estruturalpor
dc.titleA new function of ROD1 in nonsense-mediated mRNA decaypor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage1110por
oaire.citation.startPage1101por
oaire.citation.titleFEBS Letterspor
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor

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