NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10

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R-HSA-933543
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Pathway
Species
Homo sapiens
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Rotavirus, Influenza A virus, Hepatitis C Virus, Measles virus
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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) strongly 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 a scaffolding and allow the recruitment of the IKK complex in association with other signaling molecules.

Literature References
PubMed ID Title Journal Year
16127453 IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction

Kawai, T, Takahashi, K, Sato, S, Coban, C, Kumar, H, Kato, H, Ishii, KJ, Takeuchi, O

Nat Immunol 2005
16585540 Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA

Takahashi, K, Kawai, T, Kumar, H, Sato, S, Yonehara, S, Akira, S

J Immunol 2006
16618810 Caspases leave the beaten track: caspase-mediated activation of NF-kappaB

Lamkanfi, M, Declercq, W, Vanden Berghe, T, Vandenabeele, P

J Cell Biol 2006
12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and IKKalpha kinases

Shikama, Y, Yamada, M, Miyashita, T

Eur J Immunol 2003
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