◀ Back to CASP10
CASP10 — CASP8
Pathways - manually collected, often from reviews:
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
Caspase 3 (CASP3)
→
DR4/5/Caspase 8/Caspase 10/APO-2L complex (TNFRSF10B_TNFRSF10A-CASP8-CASP10-TNFSF10)
(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)
→
APO-3L (TNFSF12)
(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)
→
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 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 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)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR4/5/Caspase 8/Caspase 10 complex (TNFRSF10B_TNFRSF10A-CASP8-CASP10)
→
APO-2L (TNFSF10)
(modification, collaborate)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
DR4/5/Caspase 8/Caspase 10 complex (TNFRSF10B_TNFRSF10A-CASP8-CASP10)
→
DR4/5/Caspase 8/Caspase 10/APO-2L complex (TNFRSF10B_TNFRSF10A-CASP8-CASP10-TNFSF10)
(modification, collaborate)
-
BioCarta induction of apoptosis through dr3 and dr4/5 death receptors:
APO-2L (TNFSF10)
→
DR4/5/Caspase 8/Caspase 10/APO-2L complex (TNFRSF10B_TNFRSF10A-CASP8-CASP10-TNFSF10)
(modification, collaborate)
-
KEGG RIG-I-like receptor signaling pathway:
FADD
→
Complex of CASP10-CASP8
(protein-protein, activation)
-
KEGG RIG-I-like receptor signaling pathway:
Complex of CASP10-CASP8
→
Complex of CHUK-IKBKB-IKBKG
(protein-protein, activation)
-
KEGG Tuberculosis:
CASP8
→
CASP10
(protein-protein, activation)
-
Reactome Reaction:
CASP8
→
CASP10
(reaction)
Wang et al., Proc Natl Acad Sci U S A 2001, Shikama et al., Eur J Immunol 2003, Takahashi et al., J Immunol 2006, Lamkanfi et al., J Cell Biol 2006, Maelfait et al., Biochem Pharmacol 2008
-
WikiPathways RIG-I-like Receptor Signaling:
Complex of CASP8-CASP10
→
Complex of IKBKG-CHUK-IKBKB
(activation)
-
WikiPathways RIG-I-like Receptor Signaling:
Complex of FADD-RIPK1
→
Complex of CASP8-CASP10
(activation)
-
WikiPathways Apoptosis Modulation and Signaling:
CASP10
→
CASP8
(unknown)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(direct interaction, enzymatic study)
Srinivasula et al., Proc Natl Acad Sci U S A 1996
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(direct interaction, enzymatic study)
Guo et al., J Biol Chem 2002
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(physical association, affinity chromatography technology)
Micheau et al., Cell 2003
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(physical association, affinity chromatography technology)
Sinha et al., J Biol Chem 2004*
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(association, biochemical)
Gajate et al., J Biol Chem 2005
-
IRef Biogrid Interaction:
CASP8
—
CASP10
(physical association, affinity chromatography technology)
Lee et al., Nature communications 2012
-
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
-
IRef Hprd Interaction:
Complex of 17 proteins
MacFarlane et al., J Biol Chem 1997
-
IRef Hprd Interaction:
Complex of 17 proteins
MacFarlane et al., J Biol Chem 1997
-
IRef Hprd Interaction:
Complex of 17 proteins
MacFarlane et al., J Biol Chem 1997
-
IRef Hprd Interaction:
Complex of 19 proteins
(in vivo)
Sprick et al., EMBO J 2002*, Micheau et al., Cell 2003
-
IRef Hprd Interaction:
CASP8
—
CASP10
(in vitro)
Wang et al., Proc Natl Acad Sci U S A 2001, Sprick et al., EMBO J 2002*, Micheau et al., Cell 2003, Feig et al., EMBO J 2007*, DuBridge et al., Mol Cell Biol 1987*
-
IRef Hprd Interaction:
CASP8
—
CASP10
(in vivo)
Wang et al., Proc Natl Acad Sci U S A 2001, Sprick et al., EMBO J 2002*, Micheau et al., Cell 2003, Feig et al., EMBO J 2007*, DuBridge et al., Mol Cell Biol 1987*
-
IRef Innatedb Interaction:
Complex of CASP8-FADD-CFLAR-CASP10
(unknown, -)
Estornes et al., Cell Death Differ 2012
-
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 11 proteins
(association, coimmunoprecipitation)
Sprick et al., EMBO J 2002*
-
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 CASP8-CASP10-CFLAR-TRADD-TRAF2-RIPK1-FADD
(association, anti bait coimmunoprecipitation)
Micheau et al., Cell 2003
-
IRef Intact Interaction:
CASP10
—
CASP8
(direct interaction, fluorescent resonance energy transfer)
Wang et al., Proc Natl Acad Sci U S A 2001
-
IRef Intact Interaction:
CASP10
—
CASP8
(physical association, anti bait coimmunoprecipitation)
Feig et al., EMBO J 2007*
-
IRef Intact Interaction:
Complex of CASP10-CFLAR-CASP8
(association, anti tag coimmunoprecipitation)
Micheau et al., Cell 2003
-
IRef Ophid Interaction:
CASP10
—
CASP8
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Zhuang et al., Exp Cell Res 1999
:
Caspase-8 mediates
caspase-3 activation and cytochrome c release during singlet oxygen induced apoptosis of HL-60 cells
Raoul et al., J Cell Biol 1999
:
Motoneurons resistant to Fas activation expressed high levels of
FLICE-inhibitory protein (FLIP) , an endogenous
inhibitor of
caspase-8 activation
Okamoto et al., Rheumatology (Oxford) 2000
(Arthritis, Rheumatoid) :
Caspase-8-specific inhibitor
suppressed the activation of
caspase-3 after Fas ligation on RA synoviocytes
Hernandez et al., Surgery 2001
(Colonic Neoplasms) :
Western blots were performed to assess intracellular expression of
Flice-like inhibitory protein (FLIP) , a
caspase inhibitor
Thomas et al., Surgery 2002
(Pancreatic Neoplasms) :
FLICE-like inhibitory protein (FLIP) , an
inhibitor of
caspase-8 , ( also known as FLICE ) is regulated by the transcription factor nuclear factor-kappaB (NF-kappaB) and can contribute to TRAIL resistance
Xu et al., Anticancer Res 2003
(Pancreatic Neoplasms) :
Caspase-8 and -3 activities were increased by TRAIL treatment and apoptosis was largely
blocked by
caspase-8 and -3 inhibitors
Fujii et al., Infect Immun 2003
:
Caspase-8 is known to activate Bid, and a specific inhibitor of
caspase-8 prevented the mitochondrial damage
Perchellet et al., Anticancer Drugs 2004
:
Caspase-2 and -8 may both act upstream of mitochondria to promote Cyt c release, but
caspase-2 is already maximally
activated 6 h after 4 microM DAU or TT13 treatments, whereas DAU- or TT-induced caspase-8 and -9 activities peak at 9 h. Pre-treatments with 15 microM of the caspase-2 inhibitor benzyloxycarbonyl ( z ) -Val-Asp-Val-Ala-Asp ( VDVAD ) -fluoromethyl ketone ( fmk ) totally block DAU- and TT13 induced caspase-2, -8 and -9 activities, whereas pre-treatments with 15 microM of the caspase-8 inhibitor z-Ile-Glu-Thr-Asp ( IETD ) -fmk prevent DAU and TT13 from inducing caspase-8 activities without affecting their caspase-2- and -9-inducing activities, suggesting that the induction of apical caspase-2 activity by these drugs may be a critical upstream event required for the activation of other downstream caspases, including caspase-9 and the mitochondrial amplification loop through caspase-8
Maitra et al., Crit Care Med 2005
(Sepsis) :
Caspase-8 activates
caspase-3 , which in turn degrades fibronectin and focal adhesion kinase and leads to disruption of hepatic architecture and integrity
Miyao et al., Otol Neurotol 2006
(Cholesteatoma, Middle Ear) :
Caspase-8 , which is activated by the induction of tumor necrosis factor-alpha,
leads to activation of
caspase-3 , which activates apoptotic nucleases
Wu et al., Cell Mol Life Sci 2006
:
Caspase-8 played important roles in the activation of
caspase-3 and induction of apoptosis, whereas the role of the caspase-9 was limited
Yamaguchi et al., Biochim Biophys Acta 2006
(Carcinoma, Hepatocellular...) :
We demonstrated that
Adv-Casp8 increased expression of active forms of
caspase-8 in MOI dependent manner
Faragher et al., Mol Biol Cell 2007
(Breast Neoplasms) :
Caspase-8 activates cytoplasmic
caspase-7 , which is likely to be the primary caspase responsible for cleavage of CENP-C and INCENP, a key chromosomal passenger protein
Pesakhov et al., Nutr Cancer 2010
(Leukemia, Myeloid, Acute) :
Caspase-8 inhibition abrogated Bid cleavage and strongly
reduced caspase-9 activation, suggesting that the cross-talk mechanism mediated by caspase-8 dependent Bid cleavage can contribute to the activation of the intrinsic apoptotic pathway by curcumin + carnosic acid
Moujalled et al., Cell Death Differ 2012
:
In mouse embryonic fibroblasts, neither caspase-8 nor cellular
FLICE-inhibitory protein (FLIP) is necessary for TNF to activate NF-?B, but
caspase-8 is
required for TNF to cause cell death, and induction of FLIP by NF-?B is required to prevent it
Sata et al., J Biol Chem 1998
:
Here, we show that endothelial cell apoptosis by OxLDL and LPC-C16 : 0 was dose dependent and correlated with down-regulation of
FLICE-inhibitory protein (FLIP) , an intracellular
caspase inhibitor
Yamashita et al., Blood 1999
:
Caspase-8 activated
caspase-3 and T18 in neutrophil cytoplasmic extracts