FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex

Muzio, Marta; Chinnaiyan, Arul M; Kischkel, Frank C; O'Rourke, Karen; Shevchenko, Andrej; Ni, Jian; Scaffidi, Carsten; Bretz, James D; Zhang, Mei; Gentz, Reiner; Mann, Matthias; Krammer, Peter H; Peter, Marcus E; Dixit, Vishva M

doi:10.1016/s0092-8674(00)81266-0

Cited by 3,046Cell death mechanisms and regulationCancer-related Molecular PathwaysNF-κB Signaling Pathways

FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex

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Muzio, Marta, Chinnaiyan, Arul M, Kischkel, Frank C, O'Rourke, Karen, Shevchenko, Andrej, Ni, Jian, Scaffidi, Carsten, Bretz, James D +6 more·1996·Cell

DOI 10.1016/s0092-8674(00)81266-0

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Abstract

To identify CAP3 and CAP4, components of the CD95 (Fas/APO-1) death-inducing signaling complex, we utilized nano-electrospray tandem mass spectrometry, a recently developed technique to sequence femtomole quantities of polyacrylamide gel-separated proteins. Interestingly, CAP4 encodes a novel 55 kDa protein, designated FLICE, which has homology to both FADD and the ICE/CED-3 family of cysteine proteases. FLICE binds to the death effector domain of FADD and upon overexpression induces apoptosis that is blocked by the ICE family inhibitors, CrmA and z-VAD-fmk. CAP3 was identified as the FLICE prodomain which likely remains bound to the receptor after proteolytic activation. Taken together, this is unique biochemical evidence to link a death receptor physically to the proapoptotic proteases of the ICE/CED-3 family.

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Death receptor ligation generally allows assembly of a dynamic multiprotein complex at the intracellular tail (DISC, complex I, complex II) that regulates CASP8 (or CASP10) activation.
“As a general rule, death receptor ligation allows for the assembly of a dynamic multiprotein complex at the intracellular tail of the receptor, such as so-called “death-inducing signaling complex” (DISC), “complex I”, and “complex II”, which operate as molecular platforms to regulate the activation and functions of CASP8 (or CASP10, in a limited number of settings) [274–276].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [276]

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Authors: Muzio, M., Chinnaiyan, A. M., Kischkel, F. C., O'Rourke, K., Shevchenko, A., Ni, J., Scaffidi, C., Bretz, J. D., Zhang, M., Gentz, R., Mann, M., Krammer, P. H., Peter, M. E., & Dixit, V. M.
Affiliations: University of Michigan (US)
German Cancer Research Center (DE)
European Molecular Biology Laboratory (DE)
Human Genome Sciences (United States) (US)
Corresponding author: Dixit, Vishva M
ORCID: Muzio, Marta
Chinnaiyan, Arul M
Shevchenko, Andrej
Ni, Jian
Bretz, James D
Zhang, Mei
Mann, Matthias
Krammer, Peter H
Peter, Marcus E
Dixit, Vishva M
Venue: Cell
Publisher: Elsevier BV
Published: 1996-06
Volume: 85
Issue: 6
Pages: 817-827
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)81266-0
OpenAlex: W2094334993
Cited by: 3,046
References: 72
Citations by year: 2026: 25 · 2025: 24 · 2024: 23 · 2023: 35 · 2022: 34 · 2021: 30 · 2020: 31 · 2019: 29 · 2018: 26 · 2017: 40 · 2016: 35 · 2015: 38 · 2014: 50 · 2013: 52 · 2012: 44
FWCI: 120.57
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6286 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: caspase-8, FADD, Fas, death-inducing signaling complex, apoptosis, death effector domain, CrmA, z-VAD-fmk, proteolytic activation
MeSH terms: Amino Acid Sequence, Breast Neoplasms, Carcinoma, Carrier Proteins, Cysteine Endopeptidases, Humans, Molecular Sequence Data, Organ Specificity, Protein Binding, RNA, Messenger, Serine Endopeptidases, Tumor Cells, Cultured, Signal Transduction, Helminth Proteins, Cysteine Proteinase Inhibitors, Apoptosis, Sequence Homology, Amino Acid, Sequence Analysis, fas Receptor, Caspases, Caenorhabditis elegans Proteins, Adaptor Proteins, Signal Transducing, Caspase 8, Fas-Associated Death Domain Protein, Caspase 9, Granzymes

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FLICE, A Novel FADD-Homologous ICE/CED-3–like Protease, Is Recruited to the CD95 (Fas/APO-1) Death-Inducing Signaling Complex

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