IPS-1 interacts with RIP-1 and FADD Processing of caspases Recruitment of IKK complex Recruitment of caspase-8 and -10 to FADD complex Dimerzation of procaspase-8/10 PathwayStep6937 PathwayStep6938 PathwayStep6935 PathwayStep6936 PathwayStep6934 NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 Authored: Garapati, P V, 2010-08-02 Edited: Garapati, P V, 2010-08-02 Fas-associateddeathdomain (FADD) and receptor interacting protein 1 (RIP1) are death domain containing molecules that interact with the C-terminal portion of IPS-1 and induce NF-kB through interaction and activation of initiator caspases (caspase-8 and -10). Caspases are usually involved in apoptosis and inflammation but they also exhibit nonapoptotic functions. These nonapoptotic caspase functions involve prodomain-mediated activation of NF-kB. Processed caspases (caspase-8/10) encoding the DED (death effector domain)starongly activate NF-kB. The exact mechanism by which caspases mediate NF-kB activation is unclear but the prodomains of caspase-8/10 may act as scaffolding and allow the recruitment of IKK complex in proximity with other signaling molecules. Pubmed12884866 Pubmed16127453 Pubmed16585540 Pubmed16618810 Reactome Database ID Release 43933543 Reactome, http://www.reactome.org ReactomeREACT_25039 Reviewed: Kawai, T, Akira, S, 2010-10-30