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http://purl.uniprot.org/citations/15200957http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200957http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15200957http://www.w3.org/2000/01/rdf-schema#comment"Apoptotic cell death and survival is controlled by pro- and antiapoptotic proteins. Because these proteins act on each other, cell fate is dictated by the relative activity of pro-versus antiapoptotic proteins. Here we report that BRUCE, a conserved 528 kDa peripheral membrane protein of the trans-Golgi network, protects cells against apoptosis and functions as an inhibitor of apoptosis (IAP). By using wild-type and mutant forms we show that BRUCE inhibits caspase activity and apoptosis depending on its BIR domain. Upon apoptosis induction, BRUCE is antagonized by three mechanisms: first, through binding to Smac; second, by the protease HtrA2; and third, by caspase-mediated cleavage. In addition to its IAP activity BRUCE has the distinctive property of functioning as a chimeric E2/E3 ubiquitin ligase with Smac being a substrate. Our work suggests that, owing to its two activities and its localization, BRUCE may function as a specialized regulator of cell death pathways."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.05.018"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2004.05.018"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Pohl C."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Pohl C."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Jentsch S."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Jentsch S."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Pyrowolakis G."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Pyrowolakis G."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Bartke T."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/author"Bartke T."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/pages"801-811"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/pages"801-811"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/title"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/title"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase."xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15200957http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/15200957http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15200957
http://purl.uniprot.org/citations/15200957http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15200957