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http://purl.uniprot.org/citations/14636577http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14636577http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14636577http://www.w3.org/2000/01/rdf-schema#comment"Eukaryotic mRNAs containing premature termination codons (PTCs) are degraded by a process known as nonsense-mediated mRNA decay (NMD). NMD has been suggested to require the recognition of PTC by an mRNA surveillance complex containing UPF1/SMG-2. In multicellular organisms, UPF1/SMG-2 is a phosphoprotein, and its phosphorylation contributes to NMD. Here we show that phosphorylated hUPF1, the human ortholog of UPF1/SMG-2, forms a complex with human orthologs of the C. elegans NMD proteins SMG-5 and SMG-7. The complex also associates with protein phosphatase 2A (PP2A), resulting in dephosphorylation of hUPF1. Overexpression of hSMG-5 mutants that retain interaction with P-hUPF1 but which cannot induce its dephosphorylation impair NMD, suggesting that NMD requires P-hUPF1 dephosphorylation. We also show that P-hUPF1 forms distinct complexes containing different isoforms of hUPF3A. We propose that sequential phosphorylation and dephosphorylation of hUPF1 by hSMG-1 and PP2A, respectively, contribute to the remodeling of the mRNA surveillance complex."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(03)00443-x"xsd:string
http://purl.uniprot.org/citations/14636577http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(03)00443-x"xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Ohno S."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Ohno S."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Yamashita A."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Yamashita A."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Ohnishi T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Ohnishi T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Hentze M.W."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Kashima I."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Kashima I."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Hachiya T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Hachiya T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Anders K.R."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Anders K.R."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Anderson P."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Anderson P."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Schell T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Schell T."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Grimson A."xsd:string
http://purl.uniprot.org/citations/14636577http://purl.uniprot.org/core/author"Grimson A."xsd:string