◀ Back to CASP8
CASP8 — FADD
Pathways - manually collected, often from reviews:
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OpenBEL Selventa BEL large corpus:
Complex of CASP8-FADD-IKBKG-RALBP1-TRAF2
→
TNFSF10
(increases)
Varfolomeev et al., J Biol Chem 2005*
Evidence: Here we show that Apo2L/TRAIL activates kinase pathways by promoting the association of a secondary signaling complex, subsequent to assembly of a primary, death-inducing signaling complex (DISC). The secondary complex retained the DISC components FADD and caspase-8, but recruited several factors involved in kinase activation by TNF, namely, RIP1, TRAF2, and NEMO/IKKgamma.
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OpenBEL Selventa BEL large corpus:
CASP8
→
Complex of CASP8-FADD-FAS
(directlyIncreases, CASP8/FADD/FAS Activity)
Evidence: a dimeric Smac/DIABLO molecule is required for binding to BIR2, but not to BIR3, which indicates significant differences in the affinity or mechanism by which Smac/DIABLO binds to these domains Figure 5: Association of IAPs with signalling complexes.
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OpenBEL Selventa BEL large corpus:
CASP8
→
FADD
(increases, FADD Activity)
Evidence: the death receptor pahtway activates casp8 and also casp10 via the adaptor protein FADD
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BioCarta hiv-1 nef: negative effector of fas and tnf:
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8/FAS L complex (FAS-FADD-DAXX-MAP3K5-CASP8-FASLG)
→
Caspase 8/Caspase 8/Caspase 8/Caspase 8 complex (CASP8)
(modification, activates)
-
BioCarta hiv-1 nef: negative effector of fas and tnf:
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8/FAS L complex (FAS-FADD-DAXX-MAP3K5-CASP8-FASLG)
→
I-FLICE (CFLAR)
(modification, activates)
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BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10/APO-3L complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10-TNFSF12)
→
APO-3L (TNFSF12)
(modification, collaborate)
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BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10/APO-3L complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10-TNFSF12)
→
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10 complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10)
(modification, collaborate)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
APO-3L (TNFSF12)
→
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10 complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10)
(modification, collaborate)
-
BioCarta tnfr1 signaling pathway:
TNF-alpha/TNF R1/RIP/RAIDD/MADD/TRADD/TRAF2/cIAP complex (TNF-CRADD-TRAF2-BIRC3-TNFRSF1A-MADD-RIPK1-TRADD)
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, activates)
-
BioCarta tnfr1 signaling pathway:
FADD
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, collaborate)
-
BioCarta tnfr1 signaling pathway:
FADD
→
Caspase 8 (CASP8)
(modification, collaborate)
-
BioCarta tnfr1 signaling pathway:
FADD/Caspase 8 complex (CASP8-FADD)
→
Caspase 8 (CASP8)
(modification, collaborate)
-
BioCarta hiv-1 nef: negative effector of fas and tnf:
TNFSF6 (FASLG)
→
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8 complex (FAS-FADD-DAXX-MAP3K5-CASP8)
(modification, collaborate)
-
BioCarta hiv-1 nef: negative effector of fas and tnf:
TNFSF6 (FASLG)
→
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8/FAS L complex (FAS-FADD-DAXX-MAP3K5-CASP8-FASLG)
(modification, collaborate)
-
BioCarta hiv-1 nef: negative effector of fas and tnf:
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8 complex (FAS-FADD-DAXX-MAP3K5-CASP8)
→
FAS/FADD/DAXX/ASK1/Caspase 8/Caspase 8/FAS L complex (FAS-FADD-DAXX-MAP3K5-CASP8-FASLG)
(modification, collaborate)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10/APO-3L complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10-TNFSF12)
→
Caspase 3 (CASP3)
(modification, activates)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10/APO-3L complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10-TNFSF12)
→
Caspase 3 (active) (CASP3)
(modification, activates)
-
BioCarta ceramide signaling pathway:
FADD
→
Caspase 8 (CASP8)
(modification, collaborate)
-
BioCarta ceramide signaling pathway:
FADD
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, collaborate)
-
BioCarta ceramide signaling pathway:
Caspase 8 (CASP8)
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, collaborate)
-
BioCarta ceramide signaling pathway:
FADD/Caspase 8 complex (CASP8-FADD)
→
TNF/TNF R/TRADD/MADD/cIAP/RIP/TRAF2/RAIDD complex (TRADD-MADD-BIRC3-RIPK1-TRAF2-CRADD-TNFRSF1A-TNF)
(modification, collaborate)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR3/TRADD/FADD/TRAF2/RIP/Caspase 8/Caspase 10/APO-3L complex (TNFRSF25-TRADD-FADD-TRAF2-RIPK1-CASP8-CASP10-TNFSF12)
→
MAP3K14
(modification, activates)
-
KEGG Apoptosis:
FADD
→
CASP8
(protein-protein, activation)
-
KEGG Apoptosis:
FADD
→
CASP8
(protein-protein, activation)
-
KEGG Apoptosis:
FADD
→
CASP8
(protein-protein, activation)
-
KEGG Toll-like receptor signaling pathway:
FADD
→
CASP8
(protein-protein, activation)
-
KEGG RIG-I-like receptor signaling pathway:
FADD
→
Complex of CASP10-CASP8
(protein-protein, activation)
-
KEGG Alzheimer's disease:
FADD
→
CASP8
(protein-protein, activation)
-
KEGG Chagas disease (American trypanosomiasis):
FADD
→
CASP8
(protein-protein, activation)
-
KEGG Tuberculosis:
Complex of FADD-TRADD
→
CASP8
(protein-protein, activation)
-
KEGG Pathways in cancer:
FADD
→
CASP8
(protein-protein, activation)
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
TNFR1A/Caspase 2/TNF-alpha/FADD/TRADD/RIP/cIAP2/TRAF1/TRAF2/Ask1/RAIDD complex (TNFRSF1A-CASP2-TNF-FADD-TRADD-RIPK1-MAP3K5-TRAF1-TRAF2-BIRC3-CRADD)
→
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8/FASLG complex (FASLG-CASP8-MAP3K5-FAS-DAXX-FADD)
(modification, activates)
Micheau et al., Cell 2003, Yang et al., Cell 1997, Saitoh et al., EMBO J 1998, Chang et al., Science 1998
-
NCI Pathway Database TRAIL signaling pathway:
Caspase 8 (CASP8)
→
TRAIL/TRAILR2/FADD complex (TNFRSF10B-FADD-TNFSF10)
(modification, collaborate)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Ganten et al., Cell Death Differ 2004, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database TRAIL signaling pathway:
TRAIL/TRAILR2/FADD complex (TNFRSF10B-FADD-TNFSF10)
→
Caspase 8 (tetramer) complex (CASP8)
(modification, activates)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Ganten et al., Cell Death Differ 2004, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
BID (BID)
→
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
(modification, collaborate)
Luo et al., Cell 1998*, Li et al., Cell 1998*
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
p15 BID (BID)
(modification, activates)
Luo et al., Cell 1998*, Li et al., Cell 1998*
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
p13 BID (BID)
(modification, activates)
Luo et al., Cell 1998*, Li et al., Cell 1998*
Evidence: mutant phenotype, assay
-
NCI Pathway Database Ceramide signaling pathway:
FADD (FADD)
→
Caspase 8 (CASP8)
(modification, collaborate)
Boldin et al., Cell 1996, Muzio et al., Cell 1996
Evidence: assay
-
NCI Pathway Database Ceramide signaling pathway:
FADD (FADD)
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, collaborate)
Boldin et al., Cell 1996, Muzio et al., Cell 1996
Evidence: assay
-
NCI Pathway Database Ceramide signaling pathway:
Caspase 8 (CASP8)
→
FADD/Caspase 8 complex (CASP8-FADD)
(modification, collaborate)
Boldin et al., Cell 1996, Muzio et al., Cell 1996
Evidence: assay
-
NCI Pathway Database Ceramide signaling pathway:
FADD/Caspase 8 complex (CASP8-FADD)
→
TNF-alpha/TNFR1A/TRADD/MADD/cIAP2/RIP/TRAF2/RAIDD complex (TRADD-MADD-BIRC3-RIPK1-TRAF2-CRADD-TNFRSF1A-TNF)
(modification, collaborate)
Boldin et al., Cell 1996, Muzio et al., Cell 1996
Evidence: assay
-
NCI Pathway Database Caspase Cascade in Apoptosis:
sTNF-alpha/TNFR1A/TRADD/TRAF2/FADD complex (TNFRSF1A-TRADD-TRAF2-FADD-TNF)
→
Caspase 8 (CASP8)
(modification, activates)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Schneider-Brachert et al., Immunity 2004, Schneider-Brachert et al., J Clin Invest 2006, Lavrik et al., J Biol Chem 2008, Boldin et al., Cell 1996, Walczak et al., EMBO J 1997, Scaffidi et al., EMBO J 1998
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
FASLG (FASLG)
→
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8 complex (FAS-FADD-DAXX-MAP3K5-CASP8)
(modification, collaborate)
Juo et al., Curr Biol 1998
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
FASLG (FASLG)
→
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8/FASLG complex (FASLG-CASP8-MAP3K5-FAS-DAXX-FADD)
(modification, collaborate)
Juo et al., Curr Biol 1998
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8 complex (FAS-FADD-DAXX-MAP3K5-CASP8)
→
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8/FASLG complex (FASLG-CASP8-MAP3K5-FAS-DAXX-FADD)
(modification, collaborate)
Juo et al., Curr Biol 1998
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
clathrin heavy chain (CLTC)
(translocation, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FADD/FADD/CASP8/CASP8 complex (FADD-CASP8)
(translocation, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FASLG/FAS (trimer) complex (FAS-FASLG)
(translocation, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
Ezrin (EZR)
(translocation, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
clathrin heavy chain (CLTC)
→
FADD/FADD/CASP8/CASP8 complex (FADD-CASP8)
(translocation, activates)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FADD/FADD/CASP8/CASP8 complex (FADD-CASP8)
→
FASLG/FAS (trimer) complex (FAS-FASLG)
(translocation, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Algeciras-Schimnich et al., FEBS Lett 2003, Lee et al., EMBO J 2006, Lavrik et al., J Biol Chem 2008
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database TRAIL signaling pathway:
Caspase 8 (CASP8)
→
TRAIL/TRAILR1/DAP3/GTP/FADD complex (TNFRSF10A-FADD-TNFSF10-DAP3)
(modification, collaborate)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Miyazaki et al., Nat Immunol 2001, Ganten et al., Cell Death Differ 2004, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database TRAIL signaling pathway:
TRAIL/TRAILR1/DAP3/GTP/FADD complex (TNFRSF10A-FADD-TNFSF10-DAP3)
→
Caspase 8 (tetramer) complex (CASP8)
(modification, activates)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Miyazaki et al., Nat Immunol 2001, Ganten et al., Cell Death Differ 2004, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
cIAP1-2 (BIRC2/BIRC3)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
(modification, inhibits)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
cIAP1-2 (BIRC2/BIRC3)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, inhibits)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CFLIP complex (FAS-FASLG-FADD-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
c-FLIP (CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
Caspase 8 p10 (CASP8)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CFLIP complex (FAS-FASLG-FADD-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
c-FLIP p12 (CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
c-FLIP (CFLAR)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 p10 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 p10 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CFLIP complex (FAS-FASLG-FADD-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 p10 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CFLIP complex (FAS-FASLG-FADD-CFLAR)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8 p43/c-FLIP p43 complex (FAS-FASLG-FADD-CASP8-CFLAR)
→
c-FLIP p12 (CFLAR)
(modification, collaborate)
Yeh et al., Immunity 2000, Krueger et al., J Biol Chem 2001, Algeciras-Schimnich et al., Mol Cell Biol 2002, Chang et al., EMBO J 2002, Geserick et al., J Cell Biol 2009, Muzio et al., Cell 1996, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
Caspase 3 (CASP3)
(modification, activates)
Stennicke et al., J Biol Chem 1998*
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
Caspase 3 (tetramer) complex (CASP3)
(modification, activates)
Stennicke et al., J Biol Chem 1998*
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
c-FLIPS (CFLAR)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8/c-FLIPS complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Krueger et al., J Biol Chem 2001, Chang et al., EMBO J 2002
Evidence: assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD/CASP8/c-FLIPS complex (FAS-FASLG-FADD-CASP8-CFLAR)
(modification, collaborate)
Krueger et al., J Biol Chem 2001, Chang et al., EMBO J 2002
Evidence: assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (CASP8)
→
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
(modification, collaborate)
Krueger et al., J Biol Chem 2001, Chang et al., EMBO J 2002
Evidence: assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/c-FLIPS complex (FAS-FASLG-FADD-CASP8-CFLAR)
→
FASLG/FAS (trimer)/FADD/FADD complex (FAS-FASLG-FADD)
(modification, collaborate)
Krueger et al., J Biol Chem 2001, Chang et al., EMBO J 2002
Evidence: assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
IKK complex complex (CHUK-IKBKB-IKBKG)
(modification, activates)
Kreuz et al., J Cell Biol 2004
Evidence: mutant phenotype, assay
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
c-FLIP (CFLAR)
→
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8/FASLG complex (FASLG-CASP8-MAP3K5-FAS-DAXX-FADD)
(modification, inhibits)
Medema et al., EMBO J 1997
-
NCI Pathway Database HIV-1 Nef: Negative effector of Fas and TNF-alpha:
FAS/FADD/DAXX/Ask1/Caspase 8/Caspase 8/FASLG complex (FASLG-CASP8-MAP3K5-FAS-DAXX-FADD)
→
Caspase 8 (4 units) complex (CASP8)
(modification, activates)
Medema et al., EMBO J 1997
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
(modification, inhibits)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Cursi et al., EMBO J 2006*, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FADD/FADD/CASP8/CASP8 complex (FADD-CASP8)
(modification, inhibits)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Cursi et al., EMBO J 2006*, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
FADD/FADD/CASP8/CASP8 complex (FADD-CASP8)
(modification, collaborate)
Algeciras-Schimnich et al., Mol Cell Biol 2002, Cursi et al., EMBO J 2006*, Medema et al., EMBO J 1997
Evidence: mutant phenotype, assay
-
NCI Pathway Database TNF receptor signaling pathway :
sTNF-alpha/TNFR1A/TRADD/TRAF2/FADD complex (TNFRSF1A-TRADD-TRAF2-FADD-TNF)
→
Caspase 8 (CASP8)
(modification, activates)
Schneider-Brachert et al., Immunity 2004, Schneider-Brachert et al., J Clin Invest 2006, Boldin et al., Cell 1996
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database TNF receptor signaling pathway :
sTNF-alpha/TNFR1A/TRADD/TRAF2/FADD complex (TNFRSF1A-TRADD-TRAF2-FADD-TNF)
→
Caspase 8 (tetramer) complex (CASP8)
(modification, activates)
Schneider-Brachert et al., Immunity 2004, Schneider-Brachert et al., J Clin Invest 2006, Boldin et al., Cell 1996
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
(modification, inhibits)
Cursi et al., EMBO J 2006*, Lavrik et al., J Biol Chem 2008, Scaffidi et al., EMBO J 1998
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
FASLG/FAS (trimer)/FADD/FADD/CASP8/CASP8 complex (FAS-FASLG-FADD-CASP8)
→
FASLG/FAS (trimer) complex (FAS-FASLG)
(modification, inhibits)
Cursi et al., EMBO J 2006*, Lavrik et al., J Biol Chem 2008, Scaffidi et al., EMBO J 1998
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database FAS (CD95) signaling pathway:
Caspase 8 (tetramer)/FADD/FADD complex (CASP8-FADD)
→
FASLG/FAS (trimer) complex (FAS-FASLG)
(modification, collaborate)
Cursi et al., EMBO J 2006*, Lavrik et al., J Biol Chem 2008, Scaffidi et al., EMBO J 1998
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database TRAIL signaling pathway:
Caspase 8 (CASP8)
→
TRAIL/TRAILR1/DAP3/GTP/FADD complex (TNFRSF10A-FADD-TNFSF10-DAP3)
(modification, collaborate)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Tran et al., J Biol Chem 2001, Miyazaki et al., Nat Immunol 2001, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
NCI Pathway Database TRAIL signaling pathway:
TRAIL/TRAILR1/DAP3/GTP/FADD complex (TNFRSF10A-FADD-TNFSF10-DAP3)
→
Caspase 8 (tetramer) complex (CASP8)
(modification, activates)
Bodmer et al., Nat Cell Biol 2000, Sprick et al., Immunity 2000, Kischkel et al., Immunity 2000, Tran et al., J Biol Chem 2001, Miyazaki et al., Nat Immunol 2001, Jin et al., Mol Cell Biol 2006, Walczak et al., EMBO J 1997
Evidence: mutant phenotype, assay, physical interaction
-
Reactome Reaction:
FADD
→
CASP8
(reaction)
Sprick et al., Immunity 2000, Wang et al., Proc Natl Acad Sci U S A 2001, Thomas et al., J Biol Chem 2002, Kalai et al., Cell Death Differ 2002, Boatright et al., Mol Cell 2003*, Donepudi et al., Mol Cell 2003, Creagh et al., Immunol Rev 2003, Shikama et al., Eur J Immunol 2003, Micheau et al., Cell 2003, Chang et al., EMBO J 2003*, Han et al., J Biol Chem 2004, Kaiser et al., J Immunol 2005, Takahashi et al., J Immunol 2006, Lamkanfi et al., J Cell Biol 2006, Wang et al., Cell 2008*, Maelfait et al., Biochem Pharmacol 2008, Keller et al., Structure 2009, Hughes et al., Mol Cell 2009*, Oberst et al., J Biol Chem 2010, Tenev et al., Mol Cell 2011, Feoktistova et al., Mol Cell 2011, Estornes et al., Cell Death Differ 2012, Boldin et al., Cell 1996, Ashkenazi et al., Science 1998*
-
Reactome Reaction:
FADD
→
CASP8
(indirect_complex)
Sprick et al., Immunity 2000, Siegmund et al., J Biol Chem 2001, Micheau et al., J Biol Chem 2002*, Boatright et al., Mol Cell 2003*, Donepudi et al., Mol Cell 2003, Micheau et al., Cell 2003, Chang et al., EMBO J 2003*, Kreuz et al., J Cell Biol 2004, Sharp et al., J Biol Chem 2005*, Rushworth et al., Cell cycle (Georgetown, Tex.) 2008*, Wang et al., Cell 2008*, Seal et al., Exp Hematol 2008*, Hughes et al., Mol Cell 2009*, Vittori et al., Cell Biol Int 2010*, Fricker et al., J Cell Biol 2010*, Yerbes et al., Biochim Biophys Acta 2011*, Boldin et al., Cell 1996, Ashkenazi et al., Science 1998*, Scaffidi et al., J Biol Chem 1999
-
Reactome Reaction:
FADD
→
CASP8
(direct_complex)
Kalai et al., Cell Death Differ 2002, Creagh et al., Immunol Rev 2003, Han et al., J Biol Chem 2004, Kaiser et al., J Immunol 2005, Tenev et al., Mol Cell 2011, Feoktistova et al., Mol Cell 2011, Estornes et al., Cell Death Differ 2012
-
WikiPathways Alzheimers Disease:
FADD
→
CASP8
(activation)
-
WikiPathways Nanomaterial induced apoptosis:
FADD
→
CASP8
(activation)
-
WikiPathways RIG-I-like Receptor Signaling:
Complex of FADD-RIPK1
→
Complex of CASP8-CASP10
(activation)
-
WikiPathways Regulation of toll-like receptor signaling pathway:
FADD
→
CASP8
(activation)
-
WikiPathways Apoptosis Modulation and Signaling:
FADD
→
CASP8
(unknown)
-
WikiPathways Toll-like Receptor Signaling Pathway:
FADD
→
CASP8
(activation)
-
WikiPathways Apoptosis:
RIPK1/TRADD/FADD
→
CASP8
(activation)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
FADD
—
CASP8
Besnault-Mascard et al., Oncogene 2005*
-
IRef Bind_translation Interaction:
FADD
—
CASP8
(coimmunoprecipitation)
Kaufmann et al., FEBS Lett 2002*
-
IRef Bind_translation Interaction:
FADD
—
CASP8
(two hybrid)
Besnault-Mascard et al., Oncogene 2005*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Rébé et al., Blood 2007
-
IRef Biogrid Interaction:
FADD
—
CASP8
(direct interaction, two hybrid)
Boldin et al., Cell 1996
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Puliyappadamba et al., Cell reports 2013
-
IRef Biogrid Interaction:
FADD
—
CASP8
(direct interaction, two hybrid)
Wang et al., Molecular systems biology 2011
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Micheau et al., Cell 2003
-
IRef Biogrid Interaction:
FADD
—
CASP8
(association, biochemical)
Gajate et al., J Biol Chem 2005
-
IRef Biogrid Interaction:
FADD
—
CASP8
(direct interaction, pull down)
Srinivasula et al., J Biol Chem 1997*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Srinivasula et al., J Biol Chem 1997*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Henshall et al., J Neurochem 2003*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Oshima et al., Nature 2009*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Biton et al., Cell 2011*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(direct interaction, two hybrid)
Thomas et al., J Biol Chem 2002
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Ikner et al., J Biol Chem 2011*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Mahul-Mellier et al., Cell Death Differ 2012
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Tenev et al., Mol Cell 2011
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Ramakrishnan et al., Mol Cell 2011*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Won et al., Cell Death Differ 2010*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Ryu et al., J Biol Chem 2003*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Sinha et al., J Biol Chem 2004*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(direct interaction, pull down)
Fu et al., Oncogene 2012*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Fu et al., Oncogene 2012*
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Gonzalvez et al., Mol Cell 2012
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Lee et al., Nature communications 2012
-
IRef Biogrid Interaction:
FADD
—
CASP8
(physical association, affinity chromatography technology)
Feoktistova et al., Cell cycle (Georgetown, Tex.) 2012*
-
MIPS CORUM CASP8-FADD-MALT1-BCL10 complex:
CASP8-FADD-MALT1-BCL10 complex complex (BCL10-CASP8-FADD-MALT1)
Su et al., Science 2005
-
MIPS CORUM FAS-FADD-CASP8 complex:
FAS-FADD-CASP8 complex complex (CASP8-FADD-FAS)
Nam et al., Mol Cell 2004*
-
MIPS CORUM Death induced signaling complex II (FADD, CASP8, CFLAR), cytosolic, CD95L induced:
Death induced signaling complex II (FADD, CASP8, CFLAR), cytosolic, CD95L induced complex (CASP8-CFLAR-FADD)
Lavrik et al., J Biol Chem 2008
-
MIPS CORUM Death induced signaling complex DISC (FAS, FADD, CASP8, CFLAR), membrane-associated, CD95L induced:
Death induced signaling complex DISC (FAS, FADD, CASP8, CFLAR), membrane-associated, CD95L induced complex (CASP8-CFLAR-FADD-FAS)
Lavrik et al., J Biol Chem 2008
-
MIPS CORUM Death-inducing signaling complex DISC (type I cells associated), stimulated:
Death-inducing signaling complex DISC (type I cells associated), stimulated complex (CASP8-FADD-FAS)
Scaffidi et al., EMBO J 1998
-
MIPS CORUM FAS-FADD-CASP8-CASP10 complex:
FAS-FADD-CASP8-CASP10 complex complex (CASP10-CASP8-FADD-FAS)
Wang et al., Proc Natl Acad Sci U S A 2001
-
MIPS CORUM FAS-FADD-CASP8 complex:
FAS-FADD-CASP8 complex complex (CASP8-FADD-FAS)
Wang et al., Proc Natl Acad Sci U S A 2001
-
MIPS CORUM LRRK2-FADD-CASP8:
LRRK2-FADD-CASP8 complex (CASP8-FADD-LRRK2)
Ho et al., J Neurosci 2009*
-
IRef Corum Interaction:
Complex of FADD-CASP8
(association, coimmunoprecipitation)
Olsson et al., Oncogene 2009*
-
IRef Corum Interaction:
Complex of 16 proteins
(association, anti bait coimmunoprecipitation)
Scaffidi et al., EMBO J 1998
-
IRef Corum Interaction:
Complex of FADD-BCL10-MALT1-CASP8
(association, coimmunoprecipitation)
Su et al., Science 2005
-
IRef Dip Interaction:
Complex of CASP8-FADD-FAS-YES1
(anti bait coimmunoprecipitation)
Tauzin et al., PLoS Biol 2011*
-
IRef Dip Interaction:
Complex of FADD-CASP8-RIPK1-TNFAIP3
(anti bait coimmunoprecipitation)
Oshima et al., Nature 2009*
-
IRef Dip Interaction:
FADD
—
CASP8
(physical association, anti bait coimmunoprecipitation)
Oshima et al., Nature 2009*
-
IRef Hprd Interaction:
Complex of 50 proteins
(in vivo)
Micheau et al., Cell 2003
-
IRef Hprd Interaction:
Complex of 17 proteins
(in vivo)
Sprick et al., Immunity 2000
-
IRef Hprd Interaction:
Complex of 19 proteins
(in vivo)
Sprick et al., EMBO J 2002*, Micheau et al., Cell 2003
-
IRef Hprd Interaction:
FADD
—
CASP8
(in vivo)
Wang et al., Proc Natl Acad Sci U S A 2001, Thomas et al., J Biol Chem 2002, Feig et al., EMBO J 2007*, Yao et al., EMBO J 2007*, Boldin et al., Cell 1996
-
IRef Hprd Interaction:
FADD
—
CASP8
(in vitro)
Wang et al., Proc Natl Acad Sci U S A 2001, Thomas et al., J Biol Chem 2002, Feig et al., EMBO J 2007*, Yao et al., EMBO J 2007*, Boldin et al., Cell 1996
-
IRef Hprd Interaction:
FADD
—
CASP8
(two hybrid)
Wang et al., Proc Natl Acad Sci U S A 2001, Thomas et al., J Biol Chem 2002, Feig et al., EMBO J 2007*, Yao et al., EMBO J 2007*, Boldin et al., Cell 1996
-
IRef Innatedb Interaction:
Complex of CASP8-FADD-CFLAR-CASP10
(unknown, -)
Estornes et al., Cell Death Differ 2012
-
IRef Innatedb Interaction:
Complex of CFLAR-FADD-CASP8-CASP8-FADD-CFLAR
(unknown, -)
Estornes et al., Cell Death Differ 2012
-
IRef Innatedb Interaction:
FADD
—
CASP8
(unknown, -)
Rébé et al., Blood 2007
-
IRef Innatedb Interaction:
FADD
—
CASP8
(unknown, -)
Stegh et al., EMBO J 1998*
-
IRef Innatedb Interaction:
FADD
—
CASP8
(unknown, -)
Kaufmann et al., FEBS Lett 2002*
-
IRef Innatedb Interaction:
FADD
—
CASP8
(unknown, -)
Muppidi et al., Cell Death Differ 2006*
-
IRef Intact Interaction:
Complex of TNFRSF10B-TNFSF10-FADD-CASP8
(association, pull down)
Sprick et al., Immunity 2000
-
IRef Intact Interaction:
Complex of FADD-RIPK1-RIPK3-CASP8
(physical association, anti bait coimmunoprecipitation)
He et al., Cell 2009*
-
IRef Intact Interaction:
Complex of 21 proteins
(association, anti bait coimmunoprecipitation)
Jin et al., Cell 2009
-
IRef Intact Interaction:
Complex of 13 proteins
(association, coimmunoprecipitation)
Sprick et al., EMBO J 2002*
-
IRef Intact Interaction:
Complex of CASP8-CASP8-FADD
(association, anti tag coimmunoprecipitation)
Boldin et al., Cell 1996
-
IRef Intact Interaction:
Complex of CASP8-RIPK1-TNFRSF10A-TNFRSF10B-FADD-CFLAR
(association, anti bait coimmunoprecipitation)
Rébé et al., Blood 2007
-
IRef Intact Interaction:
Complex of CASP8-TNFRSF10A-FADD
(association, anti bait coimmunoprecipitation)
Pavet et al., Cancer Res 2010
-
IRef Intact Interaction:
Complex of CASP8-FADD-RIPK1-BIRC2
(association, anti bait coimmunoprecipitation)
Feoktistova et al., Cell cycle (Georgetown, Tex.) 2012*
-
IRef Intact Interaction:
Complex of FADD-FAS-CFLAR-CASP8
(association, anti bait coimmunoprecipitation)
Tao et al., Blood 2011
-
IRef Intact Interaction:
Complex of TRAF2-RIPK1-TRADD-FADD-CASP8-CFLAR
(association, anti bait coimmunoprecipitation)
Rébé et al., Blood 2007
-
IRef Intact Interaction:
Complex of 17 proteins
(association, anti bait coimmunoprecipitation)
Rébé et al., Blood 2007
-
IRef Intact Interaction:
Complex of CASP8-CASP8-FADD-FAS
(association, anti bait coimmunoprecipitation)
Shatnyeva et al., PloS one 2011*
-
IRef Intact Interaction:
Complex of FADD-CASP8-TNFRSF10B
(association, anti bait coimmunoprecipitation)
Pavet et al., Cancer Res 2010
-
IRef Intact Interaction:
Complex of 11 proteins
(association, anti tag coimmunoprecipitation)
Unterkircher et al., Clin Cancer Res 2011*
-
IRef Intact Interaction:
Complex of PARK7-FADD-CASP8-CASP8-FADD-PARK7-PARK7-CASP8-FADD
(association, anti bait coimmunoprecipitation)
Fu et al., Oncogene 2012*
-
IRef Intact Interaction:
Complex of FADD-CASP8-TNFRSF10B-TNFRSF10A
(association, anti bait coimmunoprecipitation)
Pavet et al., Cancer Res 2010
-
IRef Intact Interaction:
Complex of 43 proteins
(association, anti tag coimmunoprecipitation)
Bangert et al., Oncogene 2012*
-
IRef Intact Interaction:
Complex of TNFRSF10B-TNFSF10-CFLAR-CASP8-FADD-CASP10
(association, pull down)
Horova et al., FEBS J 2013
-
IRef Intact Interaction:
Complex of 13 proteins
(association, coimmunoprecipitation)
Wang et al., Proc Natl Acad Sci U S A 2001
-
IRef Intact Interaction:
Complex of LRRK2-CASP8-FADD-FADD-CASP8-LRRK2
(association, anti tag coimmunoprecipitation)
Ho et al., J Neurosci 2009*
-
IRef Intact Interaction:
Complex of TRAF2-TRAF1-TRADD-FADD-CASP8-CFLAR-BIRC2-RIPK1
(association, anti bait coimmunoprecipitation)
Micheau et al., Cell 2003
-
IRef Intact Interaction:
Complex of CASP8-CASP10-CFLAR-TRADD-TRAF2-RIPK1-FADD
(association, anti bait coimmunoprecipitation)
Micheau et al., Cell 2003
-
IRef Intact Interaction:
Complex of 16 proteins
(association, anti tag coimmunoprecipitation)
Jin et al., Cell 2009
-
IRef Intact Interaction:
Complex of FASLG-FADD-FAS-CASP8
(association, anti tag coimmunoprecipitation)
Micheau et al., Cell 2003
-
IRef Intact Interaction:
Complex of FADD-TNFSF10-FADD-TNFSF10-TNFRSF10A-CASP8-TNFRSF10A-CASP8
(association, pull down)
Sprick et al., Immunity 2000
-
IRef Intact Interaction:
Complex of 17 proteins
(association, anti bait coimmunoprecipitation)
Tao et al., Blood 2011
-
IRef Intact Interaction:
FADD
—
CASP8
(direct interaction, fluorescent resonance energy transfer)
Wang et al., Proc Natl Acad Sci U S A 2001
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, two hybrid array)
Wang et al., Molecular systems biology 2011
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, anti bait coimmunoprecipitation)
Curtin et al., Br J Cancer 2003*
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, anti tag coimmunoprecipitation)
Fu et al., Oncogene 2012*
-
IRef Intact Interaction:
FADD
—
CASP8
(direct interaction, pull down)
Fu et al., Oncogene 2012*
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, anti bait coimmunoprecipitation)
Wang et al., Cell 2008*
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, anti bait coimmunoprecipitation)
Feig et al., EMBO J 2007*
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, two hybrid)
Boldin et al., Cell 1996
-
IRef Intact Interaction:
FADD
—
CASP8
(physical association, anti tag coimmunoprecipitation)
Boldin et al., Cell 1996
-
IRef Intact Interaction:
Complex of 31 proteins
(association, anti bait coimmunoprecipitation)
Löder et al., Leukemia 2012*
-
MIPS Negatome - no physical interaction between proteins Interaction:
FADD
—
CASP8
(Absence of interaction, coimmunoprecipitation)
Curtin et al., Br J Cancer 2003*
-
IRef Ophid Interaction:
FADD
—
CASP8
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
-
IRef Ophid Interaction:
FADD
—
CASP8
(aggregation, confirmational text mining)
Thomas et al., J Biol Chem 2002
-
IRef Ophid Interaction:
FADD
—
CASP8
(aggregation, confirmational text mining)
Wang et al., Proc Natl Acad Sci U S A 2001
Text-mined interactions from Literome
Kataoka et al., Curr Biol 2000
:
Activation of Fas ( CD95 ) by its ligand ( FasL ) rapidly induces cell death through recruitment and
activation of
caspase-8 via the adaptor protein
Fas associated death domain protein ( FADD )
Kischkel et al., Immunity 2000
(Lymphoma, B-Cell) :
Apo2L/TRAIL induced homomeric and heteromeric complexes of DR4 and DR5 and stimulated recruitment of
FADD and
caspase-8 and caspase-8
activation in nontransfected cells
Gil et al., Oncogene 2000
:
The interferon induced protein kinase ( PKR ), triggers apoptosis through
FADD mediated
activation of
caspase 8 in a manner independent of Fas and TNF-alpha receptors
Gil et al., Apoptosis 2000
:
The pathway of PKR induced apoptosis involves
FADD activation of
caspase 8 by a mechanism independent of Fas and TNFR
Morgan et al., Cell Death Differ 2001
(Prostatic Neoplasms) :
FADD-DN induces
caspase activation in normal epithelial cells as demonstrated using a Fluorescence Resonance Energy Transfer assay that measures caspase activity in individual living cells
Gupta et al., Exp Gerontol 2002
(Lymphopenia) :
There was an increased expression of
FADD and increased
activation of
caspase 8 and caspase 3 in lymphocytes from aged humans as compared to young subjects
Yuan et al., Oncogene 2002
(Prostatic Neoplasms) :
Since in death receptor signaling,
FADD mediates activation of
caspase-8 , which in turn cleaves BID, and since caspase-8 is activated in PTEN mediated apoptosis, we examined BID cleavage in PTEN mediated apoptosis
Milner et al., Cell Death Differ 2002
(Ovarian Neoplasms) :
Induction of apoptosis by chemotherapeutic drugs : the
role of
FADD in activation of
caspase-8 and synergy with death receptor ligands in ovarian carcinoma cells
Guseva et al., Prostate 2002
(Prostatic Neoplasms) :
As predicted, overexpression of
FADD-DN prevented activation of
caspase-8 and Bid cleavage and attenuated the release of cytochrome c and activation of caspases -2, -7, and -9 ... Overexpression of FADD-DN and Bcl-2 affected the activation of caspase-3 and PARP cleavage differently :
FADD-DN attenuated the activation of
caspase-3 and PARP cleavage whereas Bcl-2 overexpression prevented caspase-3 activation and completely blocked cleavage of PARP
Rokhlin et al., Prostate 2002
(Prostatic Neoplasms) :
Transfection of
FADD-DN in LNCaP
resulted in inhibition of
caspase activation as well as in resistance to combined treatment with TRAIL and wortmannin
Chao et al., J Biol Chem 2002
:
In contrast, adenoviral expression of
FADD-wt increased apoptosis and
caspase-3 activity in CMs under both normoxic and hypoxic conditions ... Surprisingly,
FADD-dn , as well as the specific caspase-8 inhibitor benzyloxycarbonyl-IETD-fluoromethylketone also
inhibited the activation of
caspase-9 and -3 in CMs subjected to hypoxia/SD
Uno et al., Blood 2003
(Leukemia, Myelogenous, Chronic, BCR-ABL Positive...) :
Fas associated death domain protein ( FADD ) and caspase-8, components of death inducing signaling complex ( DISC ), as well as FLIP ( FLICE [ Fas associating protein with death domain-like interleukin-1 converting enzyme ] /caspase-8 inhibitory protein ), a negative
regulator of
caspase-8 , were expressed ubiquitously in Ph1 positive leukemia cell lines irrespective of their differential sensitivities to TRAIL and FasL
Jimbo et al., Exp Cell Res 2003
:
The dominant negative form of
FADD and z-VAD-fmk
inhibited caspase-8 , caspase-9, Bid processing, cytochrome c release, and DNA fragmentation induced by ER stress, suggesting that caspase-8 and caspase-9 are the main caspases involved in ER stress mediated apoptosis of P19-36/12 ( - ) cells
Storey et al., J Biol Chem 2003
:
Kv1.3 stimulation required the expression of
Fas associated death domain protein and
activation of
caspase 8, but did not require activation of caspase 3 or protein synthesis
Tai et al., Cell Death Differ 2004
:
Instead, suppression of T-cell activation in c-FLIP-transgenic T cells could be a combinatory effect of
FADD/caspase-8 dependent signals and
c-FLIP-specific activities
Karlsson et al., J Neurooncol 2004
(Glioma) :
The results were consistent with a block in the apoptotic signaling pathways of glioma cells between caspase-8 and
caspase-3 activation, and that inducible
Fadd could
induce caspase-8 independent apoptosis in some cells
Gniadecki et al., Biochem Biophys Res Commun 2004
:
We report here that disruption of lipid rafts by cholesterol depleting compounds ( methyl-beta-cyclodextrin, filipin III, cholesterol oxidase, and mevastatin ) leads to a spontaneous clustering of Fas in the non-raft compartment of the plasma membrane, formation of
Fas-FADD complexes,
activation of
caspase-8 , and apoptosis
Chandra et al., Mol Cell Biol 2004
:
Functional analyses with dominant negative mutants, small interfering RNAs, peptide inhibitors, and Fas associated death domain (FADD)- and caspase 8-deficient Jurkat T cells establish that the mitochondrion localized active
caspase 8
results mainly from the
FADD dependent and tumor necrosis factor receptor associated death domain dependent mechanisms and that caspase 8 activation plays a causal role in VP16 induced caspase 3 activation and cell death
Manabe et al., J Reprod Dev 2004
:
( 3 )
FADD activates an initiator
caspase ( procaspase-8 ; also called FLICE ), which is a bipartite molecule, containing an N-terminal death effector domain ( DED ) and a C-terminal DD. ( 4 ) Procaspase-8 begins auto-proteolytic cleavage and activation
Rudner et al., Oncogene 2005
:
Death receptor induced apoptosis is paradigmatically mediated via the recruitment of
FADD adapter molecule to the ligand/receptor complex and subsequent
activation of
caspase-8
Bender et al., Cell Death Differ 2005
:
Cytoplasmic TRADD activates apoptosis through Fas associated death domain protein ( FADD ) and
caspase-8 activation that was
blocked by caspase inhibitors or dominant negative
FADD
Fulda et al., Eur J Cancer 2005
:
While resveratrol enhanced TRAIL induced apoptosis through G1 cell cycle arrest and survivin depletion, resveratrol failed to sensitise cells with high expression levels of Bcl-2 or FADD-DN. Interestingly, overexpression of Bcl-2 or
FADD-DN did not interfere with resveratrol mediated cell cycle arrest or survivin depletion, but blocked release of cytochrome c and Smac from mitochondria into the cytosol,
enhanced caspase activation and apoptosis upon combined treatment with resveratrol and TRAIL indicating that overexpression of Bcl-2 or FADD-DN decoupled the effect of resveratrol on the cell cycle and apoptosis
Ou et al., Hum Immunol 2005
:
FADD-DN inhibited
caspase-8 activation induced by TRAIL in the transfectants of CM and NES2Y cells
Christgen et al., Cancer Lett 2005
(Pancreatic Neoplasms) :
This study investigates the role of caspase-8 and
DN-FADD , an
inhibitor of CD95 dependent
caspase-8 activation, in gemcitabine induced apoptosis of Colo357 pancreatic cancer cells
Alaoui-El-Azher et al., Cell Microbiol 2006
:
However, blocking the FasR-FasL interaction by antagonistic antibodies to FasR or to FasL had no effect on P. aeruginosa induced caspase 8 and caspase 3 activation, neither did the silencing of FasR by small interfering RNA ( siRNA ), suggesting that
caspase 8
activation through the
FADD bypasses FasR/FasL mediated signalling ... Thus,
FADD mediated
caspase 8 activation involves intracellular ExoS in an ADPRT dependent manner
Cagnol et al., Apoptosis 2006
:
However using RNA interference and ectopic expression, we demonstrated that neither
FADD nor Fas were
necessary for
caspase 8 activation and cell death
Li et al., J Cell Physiol 2006
:
Expression of dominant negative
FADD efficiently
prevented OxLDL induced apoptosis and
caspase-8 activation
Walczak et al., Methods Mol Biol 2008
:
For the CD95 and the TRAIL-R1/R2 DISCs, it is now clear that the adaptor protein
Fas associated DD protein (FADD) forms part of these complexes and is
necessary for recruitment of the proapoptotic signaling molecules
caspase-8 and caspase-10
Zhang et al., Apoptosis 2008
:
The change in
FADD levels and distribution was
dependent on
caspase-3 , caspase-8 activity and the presence of BID
Lesinski et al., Cancer Res 2008
(Carcinoma, Renal Cell...) :
These data suggest that bortezomib and IFN-alpha act through the extrinsic pathway of apoptosis via
FADD induced
caspase-8 activation to initiate cell death
Jani et al., Cell Res 2009
(Leukemia, T-Cell) :
Inhibition of MAT II and the resultant decrease in SAMe levels enhanced expression of FasL mRNA and protein, and induced DISC ( Death Inducing Signaling Complex ) formation with
FADD ( Fas associated Death Domain ) and procaspase-8 recruitment, as well as concomitant
increase in
caspase-8 activation and decrease in c-FLIP ( s ) levels
Ho et al., J Neurosci 2009
:
This pathway is activated by disease triggering mutations, which enhance the
LRRK2-FADD association and the consequent recruitment and
activation of
caspase-8
Hasegawa et al., J Immunol 2009
:
ASC mediated AP-1 activation was inhibited by chemical or protein inhibitors for caspase-8, caspase-8 targeting small interfering RNA, and p38 and JNK inhibitors, but not by a caspase-1 inhibitor, caspase-9 or
Fas associated death domain protein ( FADD ) dominant negative mutants, FADD- or RICK targeting small interfering RNAs, or a MEK inhibitor, indicating that the ASC induced AP-1 activation is mediated by caspase-8, p38, and JNK, but does not
require caspase-1 , caspase-9, FADD, RICK, or ERK
Föger et al., FEBS J 2009
(Burkitt Lymphoma) :
This inducible nuclear-cytoplasmic translocation of
FADD is
independent of CD95 internalization, formation of the death inducing signaling complex, and
caspase-8 activation
George et al., J Neurosci Res 2010
(Neuroblastoma) :
Genistein triggered the receptor mediated apoptotic pathway through upregulation of TNF-alpha, FasL, TRADD, and
FADD and
activation of
caspase-8
Sodhi et al., Toxicol Mech Methods 2004
:
UVB ( 100 mJ/cm ( 2 ) ) irradiation induced apoptosis in macrophages concurrent with expression of Fas, Fas ligand,
Fas associated death domain (FADD) ,
activation of
caspase-8 , -3 and cleavage of poly ( ADP-ribose ) polymerase ( PARP )
Shakibaei et al., Antioxid Redox Signal 2010
:
Overall, our results indicated that mitochondrial changes are early events in TNF-alpha induced apoptosis and that these mitochondrial changes require recruitment of
FADD and
caspase-8 activation , but not caspase-3 activation or RIP recruitment
Lokeshwar et al., Cancer Res 2010
(Neoplasm Invasiveness...) :
4-MU induced caspase-8, caspase-9, and
caspase-3 activation , PARP cleavage, upregulation of Fas-L, Fas,
FADD and DR4, and downregulation of bcl-2, phosphorylated bad, bcl-XL, phosphorylated Akt, phosphorylated IKB, phosphorylated ErbB2, and phosphorylated epidermal growth factor receptor
Liu et al., J Biol Chem 2010
:
FADD down-regulation neither restored viability of PILP-1 treated cells nor
attenuated production of active
caspase-8 and t-Bid in PILP-1 treated cells, suggesting that the death receptor mediated pathway was not involved in the cytotoxicity of PILP-1
Abhari et al., Oncogene 2013
:
RIP1 is
required for the formation of a
RIP1/FADD/caspase-8 complex that drives caspase-8 activation, cleavage of Bid into tBid, mitochondrial outer membrane permeabilization, full activation of caspase-3 and caspase dependent apoptosis
Basit et al., J Biol Chem 2012
(Rhabdomyosarcoma) :
Importantly, knockdown of RIP1 by RNA interference prevented the formation of the
RIP1·FADD·caspase-8 complex and inhibited subsequent
activation of
caspase-8 , -9, and -3 ; loss of mitochondrial membrane potential ; and apoptosis upon treatment with IAP inhibitor and lexatumumab
Ahmad et al., Cancer Res 1997
:
FADD engagement of caspase-8 presumably
activates this
caspase and leads to apoptosis
Vincenz et al., J Biol Chem 1997
:
Consistent with this finding,
FLICE2 is recruited to both the CD95 and p55 tumor necrosis factor receptor signaling complexes in a
FADD dependent manner
Eberstadt et al., Nature 1998
:
FADD then
activates caspase 8 ( also known as FLICE or MACH ) through an interaction between the death-effector domains of FADD and caspase 8
Faubion et al., J Clin Invest 1999
:
Collectively, these data suggest that GCDC induced hepatocyte apoptosis involves ligand independent oligomerization of Fas, recruitment of
FADD ,
activation of
caspase 8, and subsequent activation of effector proteases, including downstream caspases and cathepsin B