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http://purl.uniprot.org/citations/20347421http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20347421http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20347421http://www.w3.org/2000/01/rdf-schema#comment"We describe a mechanistic model of polyubiquitination by the SCF(beta TrCP2) E3 ubiquitin (Ub) ligase using human I kappaB alpha as a substrate. Biochemical reconstitution experiments revealed that the polyubiquitination of I kappaB alpha began with the action of the UbcH5 E2 Ub-conjugating enzyme, transferring a single Ub to I kappaB alpha K21/K22 rapidly and efficiently. Subsequently, the Cdc34 E2 functioned in the formation of polyubiquitin chains. It was determined that a Ub fused at I kappaB alpha K21 acts as a receptor, directing Cdc34 for rapid and efficient K48-linked Ub chain synthesis that depends on SCF(beta TrCP2) and the substrate's N terminus. The I kappaB alpha-linked fusion Ub appears to mediate direct contacts with Cdc34 and the SCF's RING subcomplex. Taken together, these results suggest a role for the multifaceted interactions between the I kappaB alpha K21/K22-linked receptor Ub, the SCF's RING complex, and Cdc34 approximately S approximately Ub in establishing the optimal orientation of the receptor Ub to drive conjugation."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2010.02.025"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2010.02.025"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Wu K."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Wu K."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Pan Z.Q."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Pan Z.Q."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Kovacev J."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/author"Kovacev J."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/pages"784-796"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/pages"784-796"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/title"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/title"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/20347421http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/20347421http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20347421
http://purl.uniprot.org/citations/20347421http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20347421
http://purl.uniprot.org/citations/20347421http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20347421
http://purl.uniprot.org/citations/20347421http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20347421