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http://purl.uniprot.org/citations/31230944http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31230944http://www.w3.org/2000/01/rdf-schema#comment"Ubiquitin-conjugating enzymes (E2s) govern key aspects of ubiquitin signaling. Emerging evidence suggests that the activities of E2s are modulated by posttranslational modifications; the structural underpinnings, however, are largely unclear. Here, we unravel the structural basis and mechanistic consequences of a conserved autoubiquitination event near the catalytic center of E2s, using the human anaphase-promoting complex/cyclosome-associated UBE2S as a model system. Crystal structures we determined of the catalytic ubiquitin carrier protein domain combined with MD simulations reveal that the active-site region is malleable, which permits an adjacent ubiquitin acceptor site, Lys+5, to be ubiquitinated intramolecularly. We demonstrate by NMR that the Lys+5-linked ubiquitin inhibits UBE2S by obstructing its reloading with ubiquitin. By immunoprecipitation, quantitative mass spectrometry, and siRNA-and-rescue experiments we show that Lys+5 ubiquitination of UBE2S decreases during mitotic exit but does not influence proteasomal turnover of this E2. These findings suggest that UBE2S activity underlies inherent regulation during the cell cycle."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2019.05.008"xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Yu L."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Schweimer K."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Choudhary J.S."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Lorenz S."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Diebold M."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Mansfeld J."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Dybkov O."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Roumeliotis T.I."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Sotriffer C."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Kucerova A."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/author"Liess A.K.L."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/pages"1195-1210.e7"xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/title"Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination."xsd:string
http://purl.uniprot.org/citations/31230944http://purl.uniprot.org/core/volume"27"xsd:string
http://purl.uniprot.org/citations/31230944http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31230944
http://purl.uniprot.org/citations/31230944http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31230944
http://purl.uniprot.org/uniprot/#_Q2QD04-mappedCitation-31230944http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31230944
http://purl.uniprot.org/uniprot/#_Q16763-mappedCitation-31230944http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31230944
http://purl.uniprot.org/uniprot/#_Q6NXQ4-mappedCitation-31230944http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31230944