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http://purl.uniprot.org/citations/18799579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18799579http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18799579http://www.w3.org/2000/01/rdf-schema#comment"Rotavirus nonstructural protein NSP3 interacts specifically with the 3' end of viral mRNAs, with the eukaryotic translation initiation factor eIF4G, and with RoXaN, a cellular protein of yet-unknown function. By evicting cytoplasmic poly(A) binding protein (PABP-C1) from translation initiation complexes, NSP3 shuts off the translation of cellular polyadenylated mRNAs. We show here that PABP-C1 evicted from eIF4G by NSP3 accumulates in the nucleus of rotavirus-infected cells. Through modeling of the NSP3-RoXaN complex, we have identified mutations in NSP3 predicted to interrupt its interaction with RoXaN without disturbing the NSP3 interaction with eIF4G. Using these NSP3 mutants and a deletion mutant unable to associate with eIF4G, we show that the nuclear localization of PABP-C1 not only is dependent on the capacity of NSP3 to interact with eIF4G but also requires the interaction of NSP3 with a specific region in RoXaN, the leucine- and aspartic acid-rich (LD) domain. Furthermore, we show that the RoXaN LD domain functions as a nuclear export signal and that RoXaN tethers PABP-C1 with RNA. This work identifies RoXaN as a cellular partner of NSP3 involved in the nucleocytoplasmic localization of PABP-C1."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00872-08"xsd:string
http://purl.uniprot.org/citations/18799579http://purl.org/dc/terms/identifier"doi:10.1128/jvi.00872-08"xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Brown S.C."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Brown S.C."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Arold S.T."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Arold S.T."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Becker M.M."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Becker M.M."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Vitour D."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Vitour D."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Poncet D."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Poncet D."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Baron C.H."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Baron C.H."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Bolte S."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Bolte S."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Harb M."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Harb M."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Vende P."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/author"Vende P."xsd:string
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18799579http://purl.uniprot.org/core/date"2008"xsd:gYear