Cited by 993Cell death mechanisms and regulationCancer-related Molecular PathwaysNF-κB Signaling Pathways

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A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain

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Boldin, Mark P., Varfolomeev, Eugene E., Pancer, Zeev, Mett, Igor L., Camonis, Jacques H., Wallach, David·1995·Journal of Biological Chemistry

DOI 10.1074/jbc.270.14.7795

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Abstract

Signaling for cell death by Fas/APO1 occurs via a distinct region in its intracellular domain. This region contains a conserved sequence motif, the death domain motif, that is also found in the intracellular domains of the p55 tumor necrosis factor receptor and the low affinity nerve growth factor receptor, as well as in the regulatory domain of the ankyrins. A novel protein that specifically binds to the death domain of Fas/APO1 but not to Fas/APO1 molecules with a loss of function point mutation occurring in lprcg mice was cloned by a two-hybrid screen of a HeLa cells' cDNA library. The cloned protein itself contains a death domain motif, and this region binds to the death domain of Fas/APO1, while the region upstream to the death domain prompts self-association of the protein. Induced expression of the protein results in ligand-independent triggering of cytotoxicity, suggesting that it is involved in cell death induction by Fas/APO1.

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Authors: Boldin, M. P., Varfolomeev, E. E., Pancer, Z., Mett, I. L., Camonis, J. H., & Wallach, D.
Affiliations: Weizmann Institute of Science (IL)
Inserm (FR)
Corresponding author: Wallach, David
ORCID: Boldin, Mark P.
Varfolomeev, Eugene E.
Camonis, Jacques H.
Wallach, David
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1995-04
Volume: 270
Issue: 14
Pages: 7795-7798
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.270.14.7795
OpenAlex: W1968328677
Cited by: 993
References: 27
Citations by year: 2026: 2 · 2025: 6 · 2024: 10 · 2023: 5 · 2022: 8 · 2021: 3 · 2020: 4 · 2019: 15 · 2018: 17 · 2017: 11 · 2016: 8 · 2015: 6 · 2014: 10 · 2013: 15 · 2012: 10
FWCI: 34.99
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9352 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
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: death domain, death receptor signaling, apoptosis, protein-protein interaction, p75 neurotrophin receptor, lpr mice, two-hybrid screen, protein self-association
MeSH terms: Amino Acid Sequence, Animals, Antigens, Surface, Carrier Proteins, Cloning, Molecular, HeLa Cells, Humans, Molecular Sequence Data, Proteins, Apoptosis, Sequence Homology, Amino Acid, DNA, Complementary, fas Receptor, Adaptor Proteins, Signal Transducing, Mice, Fas-Associated Death Domain Protein

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A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain

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