http://purl.uniprot.org/citations/11604410 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11604410 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11604410 | http://www.w3.org/2000/01/rdf-schema#comment | "Inhibitor of apoptosis (IAP) proteins inhibit caspases, a function counteracted by IAP antagonists, insect Grim, HID, and Reaper and mammalian DIABLO/Smac. We now demonstrate that HtrA2, a mammalian homologue of the Escherichia coli heat shock-inducible protein HtrA, can bind to MIHA/XIAP, MIHB, and baculoviral OpIAP but not survivin. Although produced as a 50-kDa protein, HtrA2 is processed to yield an active serine protease with an N terminus similar to that of Grim, Reaper, HID, and DIABLO/Smac that mediates its interaction with XIAP. HtrA2 is largely membrane-associated in healthy cells, with a significant proportion observed within the mitochondria, but in response to UV irradiation, HtrA2 shifts into the cytosol, where it can interact with IAPs. HtrA2 can, like DIABLO/Smac, prevent XIAP inhibition of active caspase 3 in vitro and is able to counteract XIAP protection of mammalian NT2 cells against UV-induced cell death. The proapoptotic activity of HtrA2 in vivo involves both IAP binding and serine protease activity. Mutations of either the N-terminal alanine of mature HtrA2 essential for IAP interaction or the catalytic serine residue reduces the ability of HtrA2 to promote cell death, whereas a complete loss in proapoptotic activity is observed when both sites are mutated."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109891200"xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109891200"xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Moritz R.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Moritz R.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Simpson R.J."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Simpson R.J."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Kaufmann H."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Kaufmann H."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Burke R."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Burke R."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Day C.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Day C.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Vaux D.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Vaux D.L."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Pakusch M."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Pakusch M."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Silke J."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Silke J."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Ekert P.G."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Ekert P.G."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Connolly L.M."xsd:string |
http://purl.uniprot.org/citations/11604410 | http://purl.uniprot.org/core/author | "Connolly L.M."xsd:string |