RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/17145966http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17145966http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17145966http://www.w3.org/2000/01/rdf-schema#comment"Enzyme specificity in vivo is often controlled by subcellular localization. Yeast Doa4, a deubiquitylating enzyme (DUB), removes ubiquitin from membrane proteins destined for vacuolar degradation. Doa4 is recruited to the late endosome after ESCRT-III (endosomal sorting complex required for transport III) has assembled there. We show that an N-terminal segment of Doa4 is sufficient for endosome association. This domain bears four conserved elements (boxes A-D). Deletion of the most conserved of these, A or B, prevents Doa4 endosomal localization. These mutants cannot sustain ubiquitin-dependent proteolysis even though neither motif is essential for deubiquitylating activity. Ubiquitin-specific processing protease 5 (Ubp5), the closest paralogue of Doa4, has no functional overlap. Ubp5 concentrates at the bud neck; its N-terminal domain is critical for this. Importantly, substitution of the Ubp5 N-terminal domain with that of Doa4 relocalizes the Ubp5 enzyme to endosomes and provides Doa4 function. This is the first demonstration of a physiologically important DUB subcellular localization signal and provides a striking example of the functional diversification of DUB paralogues by the evolution of alternative spatial signals."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200605134"xsd:string
http://purl.uniprot.org/citations/17145966http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200605134"xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Amerik A.Y."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Amerik A.Y."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Sindhi N."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/author"Sindhi N."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/pages"825-835"xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/pages"825-835"xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/title"A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/title"A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function."xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/volume"175"xsd:string
http://purl.uniprot.org/citations/17145966http://purl.uniprot.org/core/volume"175"xsd:string
http://purl.uniprot.org/citations/17145966http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17145966
http://purl.uniprot.org/citations/17145966http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17145966
http://purl.uniprot.org/citations/17145966http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17145966
http://purl.uniprot.org/citations/17145966http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17145966