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biopax3:comment |
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.,
Reviewed: Kawai, T, Akira, S, 2010-10-30
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NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10
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http://www.reactome.org/biopax/48887BiochemicalReaction2689,
http://www.reactome.org/biopax/48887BiochemicalReaction2690,
http://www.reactome.org/biopax/48887BiochemicalReaction2691,
http://www.reactome.org/biopax/48887BiochemicalReaction2692,
http://www.reactome.org/biopax/48887BiochemicalReaction2693
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biopax3:pathwayOrder |