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http://purl.uniprot.org/citations/20558726http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20558726http://www.w3.org/2000/01/rdf-schema#comment"The oncogenic protein BCL-3 activates or represses gene transcription through binding with the NF-kappaB proteins p50 and p52 and is degraded through a phospho- and GSK3-dependent pathway. However, the mechanisms underlying its degradation remain poorly understood. Yeast two-hybrid analysis led to the identification of the proteasome subunit PSMB1 as a BCL-3-associated protein. The binding of BCL-3 to PSMB1 is required for its degradation through the proteasome. Indeed, PSMB1-depleted cells are defective in degrading polyubiquitinated BCL-3. The N-terminal part of BCL-3 includes lysines 13 and 26 required for the Lys(48)-linked polyubiquitination of BCL-3. Moreover, the E3 ligase FBW7, known to polyubiquitinate a variety of substrates phosphorylated by GSK3, is dispensable for BCL-3 degradation. Thus, our data defined a unique motif of BCL-3 that is needed for its recruitment to the proteasome and identified PSMB1 as a key protein required for the proteasome-mediated degradation of a nuclear and oncogenic IkappaB protein."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m110.112128"xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Vanderplasschen A."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Bex F."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Robert I."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Chariot A."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Merville M.P."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Viatour P."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Shostak K."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Chapelle J.P."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Olivier S."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Gothot A."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/author"Keutgens A."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/pages"25831-25840"xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/title"BCL-3 degradation involves its polyubiquitination through a FBW7-independent pathway and its binding to the proteasome subunit PSMB1."xsd:string
http://purl.uniprot.org/citations/20558726http://purl.uniprot.org/core/volume"285"xsd:string
http://purl.uniprot.org/citations/20558726http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20558726
http://purl.uniprot.org/citations/20558726http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/20558726
http://purl.uniprot.org/uniprot/#_G0Z2K0-mappedCitation-20558726http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20558726
http://purl.uniprot.org/uniprot/#_A7BJS8-mappedCitation-20558726http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20558726
http://purl.uniprot.org/uniprot/#_A0A140VK45-mappedCitation-20558726http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/20558726