Recruitment of caspase-8 and -10 to FADD complex

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Influenza A virus, Human respiratory syncytial virus A, Rotavirus, Hepatitis C Virus, Measles virus
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Caspase-8 (CASP8) and caspase-10 (CASP10) are involved in RIG-I/MDA5-dependent antiviral immune responses. Caspase-8/10 activation contributes to NF-kB activation in response to viral dsRNA.
Caspase-8/10 are synthesized as zymogens (procaspases), containing a large N-terminal prodomain with two death effector domains (DED), and a C-terminal catalytic subunit composed of small and a large domain separated by a smaller linker region. FADD plays a crucial role in the recruitment and activation of procaspase-8/10. The two DED domains of procaspase-8/10 interacts with DED domain of FADD.

Literature References
PubMed ID Title Journal Year
16585540 Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA

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

J Immunol 2006
18761323 Non-apoptotic functions of caspase-8

Maelfait, J, Beyaert, R

Biochem Pharmacol 2008
11717445 Caspase-10 is an initiator caspase in death receptor signaling

Wong, W, Spencer, DM, Chun, HJ, Wang, J, Lenardo, MJ

Proc Natl Acad Sci U S A 2001
16618810 Caspases leave the beaten track: caspase-mediated activation of NF-kappaB

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

J Cell Biol 2006
12107169 Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen

Thomas, LR, Thorburn, A, Stillman, DJ

J Biol Chem 2002
12884866 Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and IKKalpha kinases

Miyashita, T, Shikama, Y, Yamada, M

Eur J Immunol 2003
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