The DOI matches its Crossref record; 81 of the 81 references it cites were found in a registry or an index.
A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.
Open accessAbstract
We have identified three new tumor necrosis factor-receptor associated factor (TRAF) domain-containing proteins in humans using bioinformatics approaches, including: MUL, the product of the causative gene in Mulibrey Nanism syndrome; USP7 (HAUSP), an ubiquitin protease; and SPOP, a POZ domain-containing protein. Unlike classical TRAF family proteins involved in TNF family receptor (TNFR) signaling, the TRAF domains (TDs) of MUL, USP7, and SPOP are located near the NH(2) termini or central region of these proteins, rather than carboxyl end. MUL and USP7 are capable of binding in vitro via their TDs to all of the previously identified TRAF family proteins (TRAF1, TRAF2, TRAF3, TRAF4, TRAF5, and TRAF6), whereas the TD of SPOP interacts weakly with TRAF1 and TRAF6 only. The TD of MUL also interacted with itself, whereas the TDs of USP7 and SPOP did not self-associate. Analysis of various MUL and USP7 mutants by transient transfection assays indicated that the TDs of these proteins are necessary and sufficient for suppressing NF-kappaB induction by TRAF2 and TRAF6 as well as certain TRAF-binding TNF family receptors. In contrast, the TD of SPOP did not inhibit NF-kappaB induction. Immunofluorescence confocal microscopy indicated that MUL localizes to cytosolic bodies, with targeting to these structures mediated by a RBCC tripartite domain within the MUL protein. USP7 localized predominantly to the nucleus, in a TD-dependent manner. Data base searches revealed multiple proteins containing TDs homologous to those found in MUL, USP7, and SPOP throughout eukaryotes, including yeast, protists, plants, invertebrates, and mammals, suggesting that this branch of the TD family arose from an ancient gene. We propose the moniker TEFs (TD-encompassing factors) for this large family of proteins.
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“Thus, truncation of amino acids 1–207 abolishes its ability to enter the nucleus.”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Zapata et al., 2001
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Metadata
- Authors
- Zapata, J. M., Pawlowski, K., Haas, E., Ware, C. F., Godzik, A., & Reed, J. C.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- La Jolla Institute for Immunology (US)
- Corresponding author
- Reed, John C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-06
- Volume
- 276
- Issue
- 26
- Pages
- 24242-24252
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1967642652
- Cited by
- 228
- References
- 80
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 7 · 2023: 4 · 2022: 8 · 2021: 4 · 2020: 11 · 2019: 8 · 2018: 9 · 2017: 7 · 2016: 6 · 2015: 5 · 2014: 6 · 2013: 16 · 2012: 13
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- AstraZeneca
- Deutsche Forschungsgemeinschaft
- National Institutes of Health (CA-69381)
- National Cancer Institute (CA 69381, P01CA069381)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Keywords
- TRAF domain, TRAF, USP7, SPOP, POZ domain, TRAF2, TRAF6, TRAF1, TRAF4, TRAF5, NF-κB signaling, protein-protein interaction, protein localization
- MeSH terms
- Tripartite Motif Proteins, Ubiquitin-Specific Peptidase 7, Amino Acid Sequence, Animals, Cytosol, Humans, Molecular Sequence Data, Nuclear Proteins, Endopeptidases, Phylogeny, Proteins, Repressor Proteins, NF-kappa B, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Receptors, Tumor Necrosis Factor, Evolution, Molecular, Jurkat Cells, Computational Biology, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, TNF Receptor-Associated Factor 1
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