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http://purl.uniprot.org/citations/18718449http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18718449http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18718449http://www.w3.org/2000/01/rdf-schema#comment"Itch, an E3 protein ubiquitin ligase (E3), which belongs to the homologous to E6-AP carboxy terminus (HECT)-type subfamily, catalyzes its own ubiquitylation. The precise nature of Itch-mediated self-modification and its biological outcome are not completely understood. Here, we show that Itch auto-ubiquitylation is an intermolecular reaction generating Lys63-linkages, rather than the Lys48-linked polyubiquitin chains that target proteins for proteasomal degradation. As a result, Itch is a relatively high stable protein, whose levels are not significantly affected by treatment by either proteasome or lysosome inhibitors. Furthermore, we demonstrate that the decay rate of a catalytic inactive Itch mutant, which is devoided of self-ubiquitylating activity, is barely indistinguishable from the one of the wild-type protein. These data definitely establish a nondegradative role for Lys63-linked Itch self-ubiquitylation."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.org/dc/terms/identifier"doi:10.1016/j.bcp.2008.07.028"xsd:string
http://purl.uniprot.org/citations/18718449http://purl.org/dc/terms/identifier"doi:10.1016/j.bcp.2008.07.028"xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Rossi M."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Rossi M."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Melino G."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Melino G."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Peschiaroli A."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Peschiaroli A."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Malatesta M."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Malatesta M."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Bernassola F."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Bernassola F."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Scialpi F."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/author"Scialpi F."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/name"Biochem. Pharmacol."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/name"Biochem. Pharmacol."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/pages"1515-1521"xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/pages"1515-1521"xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/title"Itch self-polyubiquitylation occurs through lysine-63 linkages."xsd:string
http://purl.uniprot.org/citations/18718449http://purl.uniprot.org/core/title"Itch self-polyubiquitylation occurs through lysine-63 linkages."xsd:string