| http://purl.uniprot.org/citations/12215447 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12215447 | http://www.w3.org/2000/01/rdf-schema#comment | "Death receptors, such as Fas and tumor necrosis factor-related apoptosis-inducing ligand receptors, recruit Fas-associated death domain and pro-caspase-8 homodimers, which are then autoproteolytically activated. Active caspase-8 is released into the cytoplasm, where it cleaves various proteins including pro-caspase-3, resulting in apoptosis. The cellular Fas-associated death domain-like interleukin-1-beta-converting enzyme-inhibitory protein long form (FLIP(L)), a structural homologue of caspase-8 lacking caspase activity because of several mutations in the active site, is a potent inhibitor of death receptor-induced apoptosis. FLIP(L) is proposed to block caspase-8 activity by forming a proteolytically inactive heterodimer with caspase-8. In contrast, we propose that FLIP(L)-bound caspase-8 is an active protease. Upon heterocomplex formation, a limited caspase-8 autoprocessing occurs resulting in the generation of the p43/41 and the p12 subunits. This partially processed form but also the non-cleaved FLIP(L)-caspase-8 heterocomplex are proteolytically active because they both bind synthetic substrates efficiently. Moreover, FLIP(L) expression favors receptor-interacting kinase (RIP) processing within the Fas-signaling complex. We propose that FLIP(L) inhibits caspase-8 release-dependent pro-apoptotic signals, whereas the single, membrane-restricted active site of the FLIP(L)-caspase-8 heterocomplex is proteolytically active and acts on local substrates such as RIP."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m206882200"xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Grutter M.G."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Schneider P."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Thome M."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Tschopp J."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Briand C."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Nicholson D.W."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Holler N."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/author | "Micheau O."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/pages | "45162-45171"xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/title | "The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex."xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://purl.uniprot.org/core/volume | "277"xsd:string |
| http://purl.uniprot.org/citations/12215447 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12215447 |
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