Trim24 targets endogenous p53 for degradation

Allton, Kendra; Jain, Abhinav K.; Herz, Hans-Martin; Tsai, Wen-Wei; Jung, Sung Yun; Qin, Jun; Bergmann, Andreas; Johnson, Randy L.; Barton, Michelle Craig

doi:10.1073/pnas.0813177106

Cited by 298Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysCell death mechanisms and regulation

Trim24 targets endogenous p53 for degradation

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Allton, Kendra, Jain, Abhinav K., Herz, Hans-Martin, Tsai, Wen-Wei, Jung, Sung Yun, Qin, Jun, Bergmann, Andreas, Johnson, Randy L. +1 more·2009·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0813177106PMC PMC2710642

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Abstract

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 p53, leading to ubiquitylation and degradation of p53.
“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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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: Allton, Kendra
Jain, Abhinav K.
Herz, Hans-Martin
Jung, Sung Yun
Qin, Jun
Bergmann, Andreas
Johnson, Randy L.
Barton, Michelle Craig
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
DOI: 10.1073/pnas.0813177106
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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Trim24 targets endogenous p53 for degradation

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