Cited by 228NF-κB Signaling PathwaysImmune Response and InflammationCytokine Signaling Pathways and Interactions

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A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.

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Zapata, Juan M., Pawlowski, Krzysztof, Haas, Elvira, Ware, Carl F., Godzik, Adam, Reed, John C.·2001·Journal of Biological Chemistry

DOI 10.1074/jbc.m100354200

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Abstract

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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Uren, 1996, Trends Biochem. Sci., 21, 244
Galang, 1994, Oncogene, 9, 2913
Krajewska, 1998, Am. J. Pathol., 152, 1549
Jin, 1997, Cancer Res., 57, 404
Albagli, 1995, Oncogene, 6, 1193
Holt, 1999, Curr. Biol., 2000, R5

Sorted by citations

Targeting Apoptosis Pathways in Cancer Therapy
Ghobrial, I. M., Witzig, T. E., & Adjei, A. A. (2005) · CA A Cancer Journal for Clinicians · doi:10.3322/canjclin.55.3.178 · Cited by 1,369
Tumor necrosis factor receptor-associated factors (TRAFs)
Bradley, J. R., & Pober, J. S. (2001) · Oncogene · doi:10.1038/sj.onc.1204788 · Cited by 652
Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde
Hu, M., Li, P., Li, M., Li, W., Yao, T., Wu, J.-W., Gu, W. J., Cohen, R. E., & Shi, Y. (2002) · Cell · doi:10.1016/s0092-8674(02)01199-6 · Cited by 666
Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family
Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588
NETWORK COMMUNICATIONS: Lymphotoxins, LIGHT, and TNF
Ware, C. F. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115719 · Cited by 452
Self-citation

See all 228

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.
ORCID: Zapata, Juan M.
Ware, Carl F.
Godzik, Adam
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)
DOI: 10.1074/jbc.m100354200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7062 d)
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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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains.

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