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http://purl.uniprot.org/citations/15084609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15084609http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15084609http://www.w3.org/2000/01/rdf-schema#comment"RNA helicase A (RHA) undergoes nuclear translocation via a classical import mechanism utilizing karyopherin beta. The nuclear transport domain (NTD) of RHA is known to be necessary and sufficient for its bi-directional nuclear trafficking. We report here that arginine methylation is a novel requirement for NTD-mediated nuclear import. Nuclear translocation of glutathione S-transferase (GST)-NTD fusion proteins is abrogated by arginine-methylation inhibitors. However, in vitro arginine-methylation of GST-NTD prior to injection allows the fusion protein to localize to the nucleus in the presence of methylation inhibitors. Removal of the arginine-rich C-terminal region negates the effects of the methylation inhibitors on NTD import, suggesting that methylation of the NTD C terminus the relieves the cytoplasmic retention of RHA. The NTD physically interacts with PRMT1, the major protein arginine methyltransferase. These findings provide evidence for a novel arginine methylation-dependent regulatory pathway controlling the nuclear import of RHA."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c300512200"xsd:string
http://purl.uniprot.org/citations/15084609http://purl.org/dc/terms/identifier"doi:10.1074/jbc.c300512200"xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"David M."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"David M."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Wong-Staal F."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Wong-Staal F."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Schurter B.T."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Schurter B.T."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Smith W.A."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/author"Smith W.A."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/pages"22795-22798"xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/pages"22795-22798"xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/title"Arginine methylation of RNA helicase a determines its subcellular localization."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/title"Arginine methylation of RNA helicase a determines its subcellular localization."xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15084609http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15084609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15084609
http://purl.uniprot.org/citations/15084609http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15084609