FADD, a novel death domain-containing protein, interacts with the death domain of fas and initiates apoptosis
Open accessAbstract
Using the cytoplasmic domain of Fas in the yeast two-hybrid system, we have identified a novel interacting protein, FADD, which binds Fas and Fas-FD5, a mutant of Fas possessing enhanced killing activity, but not the functionally inactive mutants Fas-LPR and Fas-FD8. FADD contains a death domain homologous to the death domains of Fas and TNFR-1. A point mutation in FADD, analogous to the lpr mutation of Fas, abolishes its ability to bind Fas, suggesting a death domain to death domain interaction. Overexpression of FADD in MCF7 and BJAB cells induces apoptosis, which, like Fas-induced apoptosis, is blocked by CrmA, a specific inhibitor of the interleukin-1 beta-converting enzyme. These findings suggest that FADD may play an important role in the proximal signal transduction of Fas.
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FAS and TRAILR ligands stabilize preformed receptor homotrimers to induce a conformational change enabling DD-dependent FADD association.
“In the case of FAS and TRAILRs, the cognate ligands—namely, FAS ligand (FASLG; also known as CD95L or APO-1L) and TNF superfamily member 10 (TNFSF10; best known as TRAIL), respectively—stabilize preformed receptor homotrimers to induce a conformational change at their intracellular tails that enables the death domain (DD)-dependent association of the adapter Fas associated via death domain (FADD)”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [278]
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- Authors
- Chinnaiyan, A. M., O'Rourke, K., Tewari, M., & Dixit, V. M.
- Affiliations
- University of Michigan (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-05
- Volume
- 81
- Issue
- 4
- Pages
- 505-512
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1986308149
- Cited by
- 2,431
- References
- 33
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 22 · 2023: 34 · 2022: 30 · 2021: 33 · 2020: 21 · 2019: 39 · 2018: 32 · 2017: 28 · 2016: 35 · 2015: 30 · 2014: 51 · 2013: 51 · 2012: 50
- FWCI
- 55.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- 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
- FADD, Fas, death domain, apoptosis, protein-protein interaction, TNF receptor 1, CrmA, interleukin-1 beta converting enzyme, signal transduction, MCF-7 cells, BJAB cells
- MeSH terms
- Amino Acid Sequence, Antigens, Surface, Base Sequence, Binding Sites, Carrier Proteins, Cell Line, Cloning, Molecular, Humans, Molecular Sequence Data, Saccharomyces cerevisiae, Viral Proteins, Signal Transduction, Serpins, Apoptosis, Point Mutation, fas Receptor, Adaptor Proteins, Signal Transducing, Fas-Associated Death Domain Protein
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