| http://purl.uniprot.org/citations/24275659 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24275659 | http://www.w3.org/2000/01/rdf-schema#comment | "Caspase-8 is now appreciated to govern both apoptosis following death receptor ligation and cell survival and growth via inhibition of the Ripoptosome. Cells must therefore carefully regulate the high level of caspase-8 activity during apoptosis versus the modest levels observed during cell growth. The caspase-8 paralogue c-FLIP is a good candidate for a molecular rheostat of caspase-8 activity. c-FLIP can inhibit death receptor-mediated apoptosis by competing with caspase-8 for recruitment to FADD. However, full-length c-FLIPL can also heterodimerize with caspase-8 independent of death receptor ligation and activate caspase-8 via an activation loop in the C terminus of c-FLIPL. This triggers cleavage of c-FLIPL at Asp-376 by caspase-8 to produce p43FLIP. The continued function of p43FLIP has, however, not been determined. We demonstrate that acute deletion of endogenous c-FLIP in murine effector T cells results in loss of caspase-8 activity and cell death. The lethality and caspase-8 activity can both be rescued by the transgenic expression of p43FLIP. Furthermore, p43FLIP associates with Raf1, TRAF2, and RIPK1, which augments ERK and NF-κB activation, IL-2 production, and T cell proliferation. Thus, not only is c-FLIP the initiator of caspase-8 activity during T cell activation, it is also an initial caspase-8 substrate, with cleaved p43FLIP serving to both stabilize caspase-8 activity and promote activation of pathways involved with T cell growth."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m113.506428"xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Koenig A."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "He Y.W."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Eriksson J.E."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Hakem R."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Asaoka T."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Fortner K.A."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Budd R.C."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Russell J.Q."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/author | "Buskiewicz I.A."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/pages | "1183-1191"xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/title | "The c-FLIPL cleavage product p43FLIP promotes activation of extracellular signal-regulated kinase (ERK), nuclear factor kappaB (NF-kappaB), and caspase-8 and T cell survival."xsd:string |
| http://purl.uniprot.org/citations/24275659 | http://purl.uniprot.org/core/volume | "289"xsd:string |
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