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http://purl.uniprot.org/citations/15545318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15545318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15545318http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitin is a small polypeptide that is conjugated to proteins and commonly serves as a degradation signal. The attachment of ubiquitin (Ub) to a substrate proceeds through a multi-enzyme cascade involving an activating enzyme (E1), a conjugating enzyme (E2), and a protein ligase (E3). We previously demonstrated that a murine E2, UbcM2, is imported into nuclei by the transport receptor importin-11. We now show that the import mechanism for UbcM2 and two other human class III E2s (UbcH6 and UBE2E2) uniquely requires the covalent attachment of Ub to the active site cysteine of these enzymes. This coupling of E2 activation and transport arises from the selective interaction of importin-11 with the Ub-loaded forms of these enzymes. Together, these findings reveal that Ub charging can function as a nuclear import trigger, and identify a novel link between E2 regulation and karyopherin-mediated transport."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200406001"xsd:string
http://purl.uniprot.org/citations/15545318http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200406001"xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Weissman A.M."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Weissman A.M."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Plafker S.M."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Plafker S.M."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Macara I.G."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Macara I.G."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Plafker K.S."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/author"Plafker K.S."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/pages"649-659"xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/pages"649-659"xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/title"Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/title"Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import."xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/15545318http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/15545318http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15545318
http://purl.uniprot.org/citations/15545318http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15545318