Recruitment of caspase-8 and -10 to FADD complex

Stable Identifier
R-HSA-933526
Type
Reaction [binding]
Species
Homo sapiens
Related Species
Rotavirus, Influenza A virus, Hepatitis C Virus, Measles virus
Compartment
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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
18761323 Non-apoptotic functions of caspase-8

Maelfait, J, Beyaert, R

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

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

Proc Natl Acad Sci U S A 2001
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
12107169 Regulation of Fas-associated death domain interactions by the death effector domain identified by a modified reverse two-hybrid screen

Thomas, LR, Stillman, DJ, Thorburn, A

J Biol Chem 2002
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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