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Trim24 targets endogenous p53 for degradation
Open accessAbstract
Numerous studies focus on the tumor suppressor p53 as a protector of genomic stability, mediator of cell cycle arrest and apoptosis, and target of mutation in 50% of all human cancers. The vast majority of information on p53, its protein-interaction partners and regulation, comes from studies of tumor-derived, cultured cells where p53 and its regulatory controls may be mutated or dysfunctional. To address regulation of endogenous p53 in normal cells, we created a mouse and stem cell model by knock-in (KI) of a tandem-affinity-purification (TAP) epitope at the endogenous Trp-53 locus. Mass spectrometry of TAP-purified p53-complexes from embryonic stem cells revealed Tripartite-motif protein 24 (Trim24), a previously unknown partner of p53. Mutation of TRIM24 homolog, bonus , in Drosophila led to apoptosis, which could be rescued by p53-depletion. These in vivo analyses establish TRIM24/bonus as a pathway that negatively regulates p53 in Drosophila . The Trim24-p53 link is evolutionarily conserved, as TRIM24 depletion in human breast cancer cells caused p53-dependent, spontaneous apoptosis. We found that Trim24 ubiquitylates and negatively regulates p53 levels, suggesting Trim24 as a therapeutic target to restore tumor suppression by p53.
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“TRIM24 can bind an acetylated peptide of the tumour suppressor p53, leading to ubiquitylation and degradation of the target 130 .”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [130]
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InfluentialTRIM24 promotes proliferation and metastasis of gastric cancer via mediating NRBP1 ubiquitination
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“TRIM24 is an oncoprotein overexpressed in many human malignancies, and its aberrant up-regulation in breast cancer was found to correlate with poor survival prognosis (5, 7, 8).”
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“18 0,57773292 O15164.TIF1A_HUMAN Transcription intermediary factor 1-alpha (Trim24) Ubiquitin ligase which ubiquitinylates p53 and negatively regulates its levels (Allton et al., 2009, Jain et al., 2014). p53 cofactor, regulates p53 binding to chromatin (Isbel et al., 2023), functions in DNAdamage…”
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Sustainable integrative cell biology: CENP-C is guilty by association
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“Allton et al. identified the tripartite family protein TRIM24 as an interacting partner of p53, leading to p53 ubiquitination and degradation [34].”
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“In addition to its reported E3 ubiquitin ligase activity [15], TRIM24 has also been reported to function as a transcriptional coactivator [16], further highlighting its pleiotropic roles in cellular regulation [17].”
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“For TRIM24 and TRIM28, the literature repeatedly converges on nodes such as p53-dependent apoptosis, inflammatory signaling, redox stress, and ferroptosis-related pathways [42,60].”
InfluentialZeng, W., Xu, K., Wang, Y., Shou, Y., Xiong, H., Liang, L., Xu, H., Liu, R., Zhang, H., & Lu, Y. (2026) · International Journal of Cancer · doi:10.1002/ijc.70565
“Moreover, TRIM24 exerts its E3 ubiquitin ligase activity via the RING domain, directly ubiquitinating and degrading p53, thereby reducing p53 protein stability [35].”
Bombyx mori p53 requires multiple domains for transcription-dependent apoptosis induction
Sugiura, W., Ikeda, M., & Hamajima, R. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154161
BindingDB Entry 50018757: PROTACs: New method to degrade transcription regulating proteins.
BindingDB (2024) · UC San Diego · doi:10.7270/q2280cvr
BindingDB (2017) · UC San Diego · doi:10.7270/q2js9s9g
BindingDB (2024) · UC San Diego · doi:10.7270/q2x352pq
Metadata
- Authors
- Allton, K., Jain, A. K., Herz, H.-M., Tsai, W.-W., Jung, S. Y., Qin, J., Bergmann, A., Johnson, R. L., & Barton, M. C.
- Affiliations
- The University of Texas MD Anderson Cancer Center (US)
- The University of Texas Health Science Center at Houston (US)
- Baylor College of Medicine (US)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2009-07-14
- Volume
- 106
- Issue
- 28
- Pages
- 11612-11616
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2710642
- OpenAlex
- W2037942882
- Cited by
- 292
- References
- 40
- Citations by year
- 2026: 7 · 2025: 24 · 2024: 8 · 2023: 25 · 2022: 15 · 2021: 20 · 2020: 23 · 2019: 12 · 2018: 17 · 2017: 23 · 2016: 15 · 2015: 13 · 2014: 16 · 2013: 11 · 2012: 28
- FWCI
- 10.48
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM081627, P01GM081627, GM068016, R01GM068016)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- TRIM24, p53, protein degradation, ubiquitination, tumor suppressor regulation, Drosophila, embryonic stem cells, tandem affinity purification, tumor suppression, breast cancer, apoptosis
- MeSH terms
- Animals, Chromatography, Gel, Drosophila, Humans, Mutation, Mass Spectrometry, Immunoblotting, Tumor Suppressor Protein p53, Apoptosis, Drosophila Proteins, Ubiquitin-Protein Ligases, Cell Line, Tumor, Chromatin Immunoprecipitation, Mice, Ubiquitination, Gene Knock-In Techniques
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