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http://purl.uniprot.org/citations/20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20388728http://www.w3.org/2000/01/rdf-schema#comment"Many proteins are regulated by ubiquitin-dependent proteolysis. Substrate ubiquitylation can be stimulated by additional post-translational modifications, including small ubiquitin-like modifier (SUMO) conjugation. The recently discovered SUMO-targeted ubiquitin ligases (STUbLs) mediate the latter effect; however, no endogenous substrates of STUbLs that are degraded under normal conditions are known. From a targeted genomic screen, we now identify the yeast STUbL Slx5-Slx8, a heterodimeric RING protein complex, as a key ligase mediating degradation of the MATalpha2 (alpha2) repressor. The ubiquitin-conjugating enzyme Ubc4 was found in the same screen. Surprisingly, mutants with severe defects in SUMO-protein conjugation were not impaired for alpha2 turnover. Unmodified alpha2 also bound to and was ubiquitylated efficiently by Slx5-Slx8. Nevertheless, when we inactivated four SUMO-interacting motifs (SIMs) in Slx5 that together account for its noncovalent SUMO binding, both in vitro Slx5-Slx8-dependent ubiquitylation and in vivo degradation of alpha2 were inhibited. These data identify alpha2 as the first native substrate of the conserved STUbLs, and demonstrate that its STUbL-mediated ubiquitylation does not require SUMO. We suggest that alpha2, and presumably other proteins, have surface features that mimic SUMO, and therefore can directly recruit STUbLs without prior SUMO conjugation."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.org/dc/terms/identifier"doi:10.1101/gad.1906510"xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/author"Xie Y."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/author"Rubenstein E.M."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/author"Matt T."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/pages"893-903"xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/title"SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor."xsd:string
http://purl.uniprot.org/citations/20388728http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/20388728http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20388728
http://purl.uniprot.org/citations/20388728http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20388728
http://purl.uniprot.org/uniprot/#_P40072-mappedCitation-20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/#_P40318-mappedCitation-20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/#_P0CY08-mappedCitation-20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/#_P15731-mappedCitation-20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/#_P32828-mappedCitation-20388728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/P32828http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/P40318http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/P40072http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/P0CY08http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20388728
http://purl.uniprot.org/uniprot/P15731http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/20388728