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http://purl.uniprot.org/citations/19506082http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19506082http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19506082http://www.w3.org/2000/01/rdf-schema#comment"Inhibitor of apoptosis (IAP) proteins are key regulators of intracellular signaling that interact with tumor necrosis factor (TNF) receptor superfamily members as well as proapoptotic molecules such as Smac/DIABLO and caspases. Whereas the X-linked IAP is an established caspase inhibitor, the protective mechanisms utilized by the cellular IAP (c-IAP) proteins are less clear because c-IAPs bind to but do not inhibit the enzymatic activities of caspases. In this study, c-IAPs are shown to be highly unstable molecules that undergo autoubiquitination. The autoubiquitination of c-IAP1 is blocked upon coexpression with TNF receptor-associated factor (TRAF) 2, and this is achieved by inhibition of the E3 ubiquitin ligase activity intrinsic to the RING of c-IAP1. Consistent with these observations, loss of TRAF2 results in a decrease in c-IAP1 levels. Stabilized c-IAP1 was found to sequester and prevent Smac/DIABLO from antagonizing X-linked IAP and protect against cell death. Therefore, this study describes an intriguing cytoprotective mechanism utilized by c-IAP1 and provides critical insight into how IAP proteins function to alter the apoptotic threshold."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.029983"xsd:string
http://purl.uniprot.org/citations/19506082http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m109.029983"xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Csomos R.A."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Csomos R.A."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Duckett C.S."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Duckett C.S."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Brady G.F."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/author"Brady G.F."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/pages"20531-20539"xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/pages"20531-20539"xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/title"Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/title"Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2."xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/19506082http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/19506082http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19506082
http://purl.uniprot.org/citations/19506082http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19506082
http://purl.uniprot.org/citations/19506082http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19506082
http://purl.uniprot.org/citations/19506082http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19506082