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http://purl.uniprot.org/citations/19410548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19410548http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19410548http://www.w3.org/2000/01/rdf-schema#comment"The dynamic and reversible process of ubiquitin modification controls various cellular activities. Ubiquitin exists as monomers, unanchored chains, or protein-conjugated forms, but the regulation of these interconversions remains largely unknown. Here, we identified a protein designated Rfu1 (regulator of free ubiquitin chains 1), which regulates intracellular concentrations of monomeric ubiquitins and free ubiquitin chains in Saccharomyces cerevisiae. Rfu1 functions as an inhibitor of Doa4, a deubiquitinating enzyme. Rapid loss of free ubiquitin chains upon heat shock, a condition in which more proteins require ubiquitin conjugation, was mediated in part by Doa4 and Rfu1. Thus, regulation of ubiquitin homeostasis is controlled by a balance between a deubiquitinating enzyme and its inhibitor. We propose that free ubiquitin chains function as a ubiquitin reservoir that allows maintenance of monomeric ubiquitins at adequate levels under normal conditions and rapid supply for substrate conjugation under stress conditions."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2009.02.028"xsd:string
http://purl.uniprot.org/citations/19410548http://purl.org/dc/terms/identifier"doi:10.1016/j.cell.2009.02.028"xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kimura Y."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kudo T."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kudo T."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Murata S."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Murata S."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kakizuka A."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Kakizuka A."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Yashiroda H."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Yashiroda H."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Koitabashi S."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/author"Koitabashi S."xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/pages"549-559"xsd:string
http://purl.uniprot.org/citations/19410548http://purl.uniprot.org/core/pages"549-559"xsd:string