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http://purl.uniprot.org/citations/12718880http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12718880http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12718880http://www.w3.org/2000/01/rdf-schema#comment"Messenger RNAs with premature translation termination codons (PTCs) are degraded by nonsense-mediated mRNA decay (NMD). In mammals, PTCs are discriminated from physiological stop codons by a process thought to involve the splicing-dependent deposition of an exon junction complex (EJC), EJC-mediated recruitment of Upf3, and Upf2 binding to the N terminus of Upf3. Here, we identify a conserved domain of hUpf3b that mediates an interaction with the EJC protein Y14. Tethered function analysis shows that the Y14/hUpf3b interaction is essential for NMD, while surprisingly the interaction between hUpf3b and hUpf2 is not. Nonetheless, hUpf2 is necessary for NMD mediated by tethered Y14. RNAi-induced knockdown and Y14 repletion of siRNA-treated cells implicates Y14 in the degradation of beta-globin NS39 mRNA and demonstrates that Y14 is required for NMD induced by tethered hUpf3b. These results uncover a direct role of Y14 in NMD and suggest an unexpected hierarchy in the assembly of NMD complexes."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(03)00142-4"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(03)00142-4"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Kulozik A.E."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Kulozik A.E."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Schell T."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Schell T."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Gehring N.H."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Gehring N.H."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Neu-Yilik G."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/author"Neu-Yilik G."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/pages"939-949"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/pages"939-949"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/title"Y14 and hUpf3b form an NMD-activating complex."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/title"Y14 and hUpf3b form an NMD-activating complex."xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/12718880http://purl.uniprot.org/core/volume"11"xsd:string