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http://purl.uniprot.org/citations/20817927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20817927http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20817927http://www.w3.org/2000/01/rdf-schema#comment"SMG-9 is part of a protein kinase complex, SMG1C, which consists of the SMG-1 kinase, SMG-8 and SMG-9. SMG1C mediated phosphorylation of Upf1 triggers nonsense-mediated mRNA decay (NMD), a eukaryotic surveillance pathway that detects and targets for degradation mRNAs harboring premature translation termination codons. Here, we have characterized SMG-9, showing that it comprises an N-terminal 180 residue intrinsically disordered region (IDR) followed by a well-folded C-terminal domain. Both domains are required for SMG-1 binding and the integrity of the SMG1C complex, whereas the C-terminus is sufficient to interact with SMG-8. In addition, we have found that SMG-9 assembles in vivo into SMG-9:SMG-9 and, most likely, SMG-8:SMG-9 complexes that are not constituents of SMG1C. SMG-9 self-association is driven by interactions between the C-terminal domains and surprisingly, some SMG-9 oligomers are completely devoid of SMG-1 and SMG-8. We propose that SMG-9 has biological functions beyond SMG1C, as part of distinct SMG-9-containing complexes. Some of these complexes may function as intermediates potentially regulating SMG1C assembly, tuning the activity of SMG-1 with the NMD machinery. The structural malleability of IDRs could facilitate the transit of SMG-9 through several macromolecular complexes."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkq749"xsd:string
http://purl.uniprot.org/citations/20817927http://purl.org/dc/terms/identifier"doi:10.1093/nar/gkq749"xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Ohno S."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Ohno S."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Yamashita A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Yamashita A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Fernandez I.S."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Fernandez I.S."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Llorca O."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Llorca O."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Arias-Palomo E."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Arias-Palomo E."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Teixido J."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Teixido J."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Bamba Y."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Bamba Y."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Bartolome R.A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Bartolome R.A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Canales M.A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/author"Canales M.A."xsd:string
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/20817927http://purl.uniprot.org/core/date"2011"xsd:gYear