Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade

@article{Juo1998EssentialRF,
  title={Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade},
  author={Peter Juo and Calvin J. Kuo and Junying Yuan and John Blenis},
  journal={Current Biology},
  year={1998},
  volume={8},
  pages={1001-1008}
}
BACKGROUND Fas (APO-1/CD95) is a member of the tumor necrosis factor receptor (TNF-R) family and induces apoptosis when crosslinked with either Fas ligand or agonistic antibody (Fas antibody). The Fas-Fas ligand system has an important role in the immune system where it is involved in the downregulation of immune responses and the deletion of peripheral autoreactive T lymphocytes. The intracellular domain of Fas interacts with several proteins including FADD (MORT-1), DAXX, RIP, FAF-1, FAP-1… Expand
The Role of c-FLIP in Modulation of CD95-induced Apoptosis*
TLDR
It is shown that c-FLIP is expressed in two isoforms, both of which, like FADD and caspase-8, are recruited to the CD95 DISC in a stimulation-dependent fashion and inhibits CD95-mediated apoptosis. Expand
FADD is required for multiple signaling events downstream of the receptor Fas.
  • P. Juo, M. Woo, +4 authors J. Blenis
  • Biology, Medicine
  • Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
  • 1999
TLDR
Data indicate that FADD is essential for multiple signaling events downstream of Fas, and implementation of the FADD mutant cell lines with wild-type FADD restored Fas-mediated apoptosis. Expand
Non-apoptotic Fas signaling.
TLDR
The similarities and differences of the molecular mechanisms of apoptotic and non-apoptotic Fas signaling are addressed and the pathways that are utilized by Fas to transduce proliferative and activating signals are poorly understood. Expand
Fas-associated Protein with Death Domain (FADD)-independent Recruitment of c-FLIPL to Death Receptor 5*
TLDR
The interaction of c-FLIPL and DR5 indicates a mechanism by which tumor selective apoptosis can be achieved through protecting normal cells from undergoing death receptor-induced apoptosis, and shows that a cellular membrane permeable version of the peptide corresponding to the DR5 binding domain of c -FLIP induces apoptosis in mammalian cells. Expand
Necrotic Death Pathway in FAS Receptor Signaling
TLDR
It is shown that the death effector domain of FADD is responsible for the FADD-mediated necrotic pathway, and the presence of z-VAD–fmk and pyrrolidine dithiocarbamate together blocked cell death, suggesting that both apoptotic and nec rotic pathways can be activated through the Fas death receptor. Expand
The recruitment of Fas-associated death domain/caspase-8 in Ras-induced apoptosis.
  • C. Y. Chen, P. Juo, +4 authors D. Faller
  • Biology, Medicine
  • Cell growth & differentiation : the molecular biology journal of the American Association for Cancer Research
  • 2001
TLDR
The results indicate that FADD/caspase-8 signaling is involved in PKC/Ras-mediated apoptosis, and JNK may be an upstream effector of caspase activation. Expand
Intracellular mechanisms of TRAIL: apoptosis through mitochondrial-dependent and -independent pathways
TLDR
The data suggest that death receptors (DR4 and DR5) and Fas receptors induced apoptosis through identical signaling pathway, and TRAIL-induced apoptosis via both mitochondrial-dependent and -independent pathways. Expand
Caspase-10-Dependent Cell Death in Fas/CD95 Signalling Is Not Abrogated by Caspase Inhibitor zVAD-fmk
TLDR
Genetic evidence is provided for the involvement of initiator caspase-10 in FasL-induced cell death and indicate that zVAD-fmk does not abrogate casp enzyme-10 processing and cytotoxicity in Fas signalling. Expand
The adaptor protein FADD and the initiator caspase-8 mediate activation of NF-κB by TRAIL
TLDR
The data establish the mechanism of TRAIL-induced NF-κB activation involving the TRAIL receptor DD, FADD and caspase-8, but not RIP1 or FLIP, and show that signaling of TRAil-induced apoptosis and NF-kkB bifurcates downstream of caspases-8. Expand
TRAF1 Is a Substrate of Caspases Activated during Tumor Necrosis Factor Receptor-α-induced Apoptosis*
TLDR
TRAF1 cleavage was markedly reduced in cells that contain little procaspase-8 protein, suggesting that this apical protease in the TNF/Fas death receptor pathway is largely responsible. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 65 REFERENCES
Apoptosis induced by a chimeric Fas/FLICE receptor: lack of requirement for Fas- or FADD-binding proteins.
TLDR
F/F induces cell death, indicating that FLICE activation is sufficient for apoptosis and does not require additional Fas- or FADD-binding proteins; and F/F bypasses proximal defects in Fas signaling that prevent FLICE recruitment or activation. Expand
FLICE Induced Apoptosis in a Cell-free System
TLDR
Remarkably, both CD95 and TNFR-1 death receptors initiate apoptosis by recruiting a novel ICE/CED-3 family member, designated FLICE/MACH, to the receptor signaling complex, which represents the apical triggering protease in the cascade. Expand
CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP.
FADD/MORT1 is a death domain (DD)-containing adaptor/signaling molecule that interacts with the intracellular DD of FAS/APO-I (CD95) and tumor necrosis factor receptor 1 and the prodomain ofExpand
Fas-mediated apoptosis and activation-induced T-cell proliferation are defective in mice lacking FADD/Mort1
TLDR
The results and the similarities between FADD−/− mice and mice lacking the β-subunit of the IL-2 receptor suggest that there is an unexpected connection between cell proliferation and apoptosis. Expand
Membrane Oligomerization and Cleavage Activates the Caspase-8 (FLICE/MACHα1) Death Signal*
  • David A. Martin, R. Siegel, Lixin Zheng, M. Lenardo
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 1998
TLDR
It is found that oligomerization at the cell membrane powerfully induces caspase-8 autoactivation and apoptosis, but apoptosis could involve a death signal conveyed by the proteolytic release of the enzyme into the cytoplasm. Expand
Comparison of apoptosis in wild-type and Fas-resistant cells: chemotherapy-induced apoptosis is not dependent on Fas/Fas ligand interactions.
TLDR
The results indicate that antineoplastic treatments induce apoptosis through a Fas-independent pathway even though Fas- and chemotherapy-induced pathways converge on common downstream apoptotic effector molecules. Expand
Lack of a role for Jun kinase and AP-1 in Fas-induced apoptosis.
TLDR
Induction of JNK activity in Jurkat cells by ligation of Fas at levels sufficient to cause cell death is likely a result, rather than a cause, of the apoptotic response, and AP-1 function is not required for Fas-induced apoptosis. Expand
Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin.
TLDR
Sentrin is a novel protein of 101 amino acids with homology to ubiquitin, Nedd8, and a Saccharomyces cerevisiae protein, Smt3, which interacts with Fas/APO-1 and TNF receptor 1 but not with FADD/MORT1 or CD40. Expand
FLICE Is Predominantly Expressed as Two Functionally Active Isoforms, Caspase-8/a and Caspase-8/b*
TLDR
A panel of monoclonal antibodies directed against all functional domains of FLICE showed that only two of the FLICE isoforms were predominantly expressed in cells of different origin and could be detected in significant amounts at the protein level. Expand
Effect of bcl-2 on Fas antigen-mediated cell death.
TLDR
The results suggest that the Fas Ag and TNF receptor may share the same signaling pathway, and that bcl-2 interferes with the apoptotic process mediated by the FasAg and T NF receptor. Expand
...
1
2
3
4
5
...