| http://purl.uniprot.org/citations/21849505 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21849505 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21849505 | http://www.w3.org/2000/01/rdf-schema#comment | "The inhibitors of apoptosis (IAPs) are critical regulators of apoptosis and other fundamental cellular processes. Many IAPs are RING domain-containing ubiquitin E3 ligases that control the stability of their interacting proteins. However, how IAP stability is regulated remains unclear. Here we report that USP19, a deubiquitinating enzyme, interacts with cellular IAP 1 (c-IAP1) and c-IAP2. Knockdown of USP19 decreases levels of both c-IAPs, whereas overexpression of USP19 results in a marked increase in c-IAP levels. USP19 effectively removes ubiquitin from c-IAPs in vitro, but it stabilizes c-IAPs in vivo mainly through deubiquitinase-independent mechanisms. The deubiquitinase activity is involved in the stabilization of USP19 itself, which is facilitated by USP19 self-association. Functionally, knockdown of USP19 enhances TNFα-induced caspase activation and apoptosis in a c-IAP1 and 2-dependent manner. These results suggest that the self-ubiquitin ligase activity of c-IAPs is inhibited by USP19 and implicate deubiquitinating enzymes in the regulation of IAP stability."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.282020"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m111.282020"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Hu S."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Hu S."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Mei Y."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Mei Y."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Yang X."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Yang X."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Hahn A.A."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/author | "Hahn A.A."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/pages | "35380-35387"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/pages | "35380-35387"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/title | "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/title | "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/volume | "286"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://purl.uniprot.org/core/volume | "286"xsd:string |
| http://purl.uniprot.org/citations/21849505 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21849505 |
| http://purl.uniprot.org/citations/21849505 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21849505 |