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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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Cited by
Sorted by citations
Items 101–200 of 298
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Dupont, S., Inui, M., & Newfeld, S. J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.037 · Cited by 41
“Tif1-a/Trim24 and KAP1/Tif1-b/Trim28 also act at the chromatin level via their PHD-Bromo domain [42,43] and have the potential to promote ubiquitylation through their RING-domain [44,45].”
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“tion and degradation of p53.[24] A recent study showed”
ResultCorp Regulates P53 in Drosophila melanogaster via a Negative Feedback Loop
Chakraborty, R., Li, Y., Zhou, L. J., & Golic, K. G. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005400 · Cited by 38
“Although Bonus and Rad6 have been identified as negative regulators of P53 in Drosophila [50,51], neither of them are transcriptional targets of P53, and are thus less similar to Mdm2 than is Corp.”
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“Recent work has determined that TIF1 ubiquitylates p53, targets it for proteasome-dependent degradation, and consequently inhibits p53-dependent apoptosis (1).”
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“For instance, Trim24 was identified as a p53-binding partner in mouse embryonic stem cells and shown to promote p53 degradation in organisms from Drosophila to human (Allton et al., 2009; Jain et al., 2014).”
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Stevens, R. V., Esposito, D., & Rittinger, K. (2019) · Life Science Alliance · doi:10.26508/lsa.201900295 · Cited by 34
“To our surprise, the RING domains of TRIM24, TRIM28, and TRIM33 were unable to promote ubiquitin discharge from the E2–Ub conjugates of UBE2D, UBE2E1, and UBE2E2, E2 conjugating enzymes that were described to work in conjunction with these TRIMs.”
BackgroundInfluentialTRIMming Type I Interferon-Mediated Innate Immune Response in Antiviral and Antitumor Defense
Wang, L., & Ning, S. (2021) · Viruses · doi:10.3390/v13020279 · Cited by 34
“TRIM24 promotes p53 ubiquitination and degradation and, in turn, is inducible by p53 [119].”
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“TRIM3 [37], TRIM23 [130], TRIM24[19], TRIM31 [35,40], TRIM32 [36], TRIM45 [131], TRIM59 [132], TRIM65 [133] and TRIM71 [60] associate with p53 and promote the ubiquitination and degradation of p53 through the RING domain.”
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“Mutation or altered function of p53 is found in more than half of all cancer cases and is highly related to different types of tumorigenesis (1, 22, 60).”
BackgroundThe Role of Tripartite Motif Family Proteins in TGF-β Signaling Pathway and Cancer
Lee, H.-J. (2018) · Journal of Cancer Prevention · doi:10.15430/jcp.2018.23.4.162 · Cited by 31
“TRIM24, as an E3 ubiquitin ligase, has also been identified as a p53-binding protein by mass spectrometry.(28) TRIM24 directly ubiquitinates p53 via RING domain and negatively regulates p53”
Backgroundp53-independent DUX4 pathology
Bosnakovski, D., Gearhart, M. D., Toso, E. A., Recht, O. O., Cucak, A., Jain, A. K., Barton, M. C., & Kyba, M. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.030064 · Cited by 29
“…iC2C12-DUX4 cells, which are immortalized mouse myoblasts engineered for doxycycline-inducible DUX4 expression, with retroviral vectors expressing several constructs known to interfere with p53: a dominant-negative p53 (R175H mutation), MDM2 (Momand et al., 1992) and TRIM24 (Allton et al., 2009).”
Self-citationPrognostic relevance of tripartite motif containing 24 expression in colorectal cancer
Wang, F., Han, Y., Yao, W., & Yu, J. (2017) · Pathology - Research and Practice · doi:10.1016/j.prp.2017.08.008 · Cited by 29
Further delineation of the clinical spectrum of de novo TRIM8 truncating mutations
Assoum, M., Lines, M. A., Elpeleg, O. N., Darmency, V., Whiting, S. E., Edvardson, S., Devinsky, O., Heinzen, E. L., Hernan, R., Antignac, C., et al. (2018) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.40357 · Cited by 29
TRIMming p53 for ubiquitination
Tai, E., & Benchimol, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905997106 · Cited by 28
“(3) in this issue of PNAS, and it turns out to be a member of the tripartite motif protein (TRIM) family, TRIM24.”
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Love, I. M., & Grossman, S. R. (2012) · Genes & Cancer · doi:10.1177/1947601912455198 · Cited by 28
“Depletion of Trim24 by shRNA in mouse embryonic stem (ES) cells resulted in increased p53 levels, as well as activation of its transcriptional targets MDM2 and p21.(73) Enhanced p53-dependent apoptosis in response to doxorubicin was also observed.”
BackgroundTRIM24 is an insulin-responsive regulator of P-bodies
Wei, W. Z., Chen, Q., Liu, M., Sheng, Y., Ouyang, Q., Feng, W., Yang, X., Ding, L., Su, S., Zhang, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31735-0 · Cited by 28
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Overexpression of TRIM24 is correlated with the progression of human cervical cancer.
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TRIM24 as an independent prognostic biomarker for prostate cancer
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“In addition, the up or downregulation of TRIM family members has been identified in several malignancies including TRIM19 in leukemia (7), TRIM24 in breast cancer (8) and TRIM25 in ovarian cancer (9).”
Narrative review of autoantibodies in idiopathic inflammatory myopathies
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“For example, transcription intermediary factor 1-alpha (TIF1-α) involves in the regulation of cell proliferation and apoptosis by ubiquitylation and by negatively regulating p53 levels (18).”
BackgroundThe polar warhead of a TRIM 24 bromodomain inhibitor rearranges a water‐mediated interaction network
Liu, J., Li, F., Bao, H., Jiang, Y., Zhang, S., Ma, R., Gao, J., Wu, J., & Ruan, K. (2017) · FEBS Journal · doi:10.1111/febs.14041 · Cited by 23
Loughland, J. R., Woodberry, T., Field, M. A., Andrew, D. W., SheelaNair, A., Dooley, N. L., Piera, K. A., Amante, F. H., Kenangalem, E., Price, R. N., et al. (2020) · Clinical & Translational Immunology · doi:10.1002/cti2.1144 · Cited by 22
“Upstream regulators predicted as inhibited included mitogen-activated protein kinase 1 (MAPK1), prostaglandin E2 receptor 4 (PTGER4), suppressor of cytokine signalling 1 (SOCS1) and interleukin 1 receptor antagonist (IL1RN), and tripartite-motif protein 24 (TRIM24), the negative regulator of p53 stability.(21) Increas…”
BackgroundSPOP-mutant prostate cancer: Translating fundamental biology into patient care
Bernasocchi, T., & Theurillat, J.-P. P. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.12.024 · Cited by 22
TRIM proteins in breast cancer: Function and mechanism
Bai, X., & Tang, J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.103 · Cited by 22
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Mutant p53 as an Antigen in Cancer Immunotherapy
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“Briefly, the following are E-3 ligases involved in p53 ubiquitin-mediated degradation that mediate the K48-linked polyubiquitination of p53, marking the protein for proteosomal degradation: MDM2, Fogol Caspase Recruitment Domain-Containing protein 16 (COP1) and Ring Finger And CHY Zinc Finger Domain Containing 1 (Pirh…”
MethodYang, T., Li, M., Li, H., Shi, P., Liu, J., & Chen, M. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.06.106 · Cited by 21
Lessons from interconnected ubiquitylation and acetylation of p53: think metastable networks
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Recent advances in epigenetic proteolysis targeting chimeras (Epi-PROTACs)
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The significance of CUX1 and chromosome 7 in myeloid malignancies
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Many Faces of TRIM Proteins on the Road from Pluripotency to Neurogenesis
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“In addition, TRIM24 binds to P53, ubiqutinates it by the RING domain, which promotes P53 degradation and thus prevents spontaneous ESCs apoptosis [38], as well as differentiation [33].”
E2 Ligase dRad6 Regulates DMP53 Turnover in Drosophila
Chen, S., Wei, H.-M., Lv, W., Wang, D.-L., & Sun, F.-L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.190314 · Cited by 21
Zhang, L., Chen, H., Ding, B., & Jiang, W. (2022) · Journal of Ovarian Research · doi:10.1186/s13048-022-00948-8 · Cited by 19
“Its N-terminal TRIM motif includes an important zinc-binding domain-the RING region, which is involved in ubiquitylation and degradation of the major transcription factor p53 [6, 7].”
BackgroundThe tripartite motif-containing 24 is a multifunctional player in human cancer
Yao, Y., Zhou, S., Yue, Y., Fu, K., & Xiao, S. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01289-3 · Cited by 20
“TRIM24 functions as a RING-domain E3 ligases targeting p53 for degradation [64].”
BackgroundFunctional divergence of a heterochromatin‐binding protein during stickleback speciation
Yoshida, K., Ishikawa, A., Toyoda, A., Shigenobu, S., Fujiyama, A., & Kitano, J. (2018) · Molecular Ecology · doi:10.1111/mec.14841 · Cited by 20
A novel TRIM family member, Trim69, regulates zebrafish development through p53‐mediated apoptosis
Han, R., Zhao, Q. S., Zong, S., Miao, S., Song, W., & Wang, L. (2016) · Molecular Reproduction and Development · doi:10.1002/mrd.22643 · Cited by 19
Adam, A. H. B., de Haan, L. H. J., Estruch, I. M., Hooiveld, G. J. E. J., Louisse, J., & Rietjens, I. M. C. M. (2020) · Cell Biology and Toxicology · doi:10.1007/s10565-020-09516-6 · Cited by 18
“Furthermore, it is reported to play a role in regulation of cell proliferation and apoptosis by regulating p53 level (Allton et al. 2009; Thenot et al. 1997).”
BackgroundTRIM24 controls induction of latent HIV-1 by stimulating transcriptional elongation
Horvath, R. M., Dahabieh, M. S., Malcolm, T., & Sadowski, I. (2023) · Communications Biology · doi:10.1038/s42003-023-04484-z · Cited by 18
“TRIM24 also has E3 ubiquitin ligase activity, and was shown to cause proteasomal mediated degradation of p53 (Allton et al, 2009) (Jain et al, 2014).”
BackgroundRecent advances in the pharmacological targeting of ubiquitin-regulating enzymes in cancer
Montagut, A. M., Armengol, M., Gorjón-de-Pablo, G., Estrada‐Tejedor, R., Borrell, J. I., & Roué, G. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.007 · Cited by 17
The role of TRIM family in metabolic associated fatty liver disease
Zhang, J., Zhang, Y., Ren, Z., Yan, D., & Li, G. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1210330 · Cited by 17
Tyr99 phosphorylation determines the regulatory milieu of tumor suppressor p73
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Differential Gene Expression Profile Induced by Valproic Acid (VPA) in Pediatric Epileptic Patients
Floriano-Sánchez, E., Brindis, F., Ortega-Cuéllar, D., Ignacio‐Mejía, I., Moreno-Arriola, E., Romero-Morelos, P., Ceballos-Vasquez, E., Córdova-Espinoza, M. G., Arregoitia-Sarabia, C. K., Sandoval‐Pacheco, R., et al. (2018) · Genes · doi:10.3390/genes9070328 · Cited by 16
“The TRIM24 gene encodes an E3 ubiquitin ligase [34], and defects in the ubiquitin proteasome system have long been implicated in the pathogenesis of neurodegenerative disorders.”
BackgroundLi, J., Wang, X., Chen, Y., Sun, X., Fu, L., Xin, Q., Zhang, H., Qin, B., Sun, N., Li, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202412378 · Cited by 16
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KRAB domain of ZFP568 disrupts TRIM28-mediated abnormal interactions in cancer cells
Kumar, J., Kaur, G., Ren, R., Lu, Y., Lin, K., Li, J., Huang, Y., Patel, A. B., Barton, M. C., Macfarlan, T. S., et al. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa007 · Cited by 16
“Consistent with TRIM24 directly ubiquitylating p53 for degradation (36,37), we observed that the levels of p53 increased along with decreased TRIM24 protein levels (Figure 4G).”
BackgroundInfluentialSelf-citationAguiar, P. D. C., & Severino, P. (2010) · Einstein (São Paulo) · doi:10.1590/s1679-45082010ao1674 · Cited by 16
“Some studies in animal models showed that a depletion of TRIM24 can lead to p53-induced apoptosis(13).”
BackgroundThe Janus Face of p53-Targeting Ubiquitin Ligases
Hao, Q., Chen, Y., & Zhou, X. Y. (2020) · Cells · doi:10.3390/cells9071656 · Cited by 16
“Promotes mtp53 degradation [83–85] RNF128 Induces ubiquitination and degradation of wtp53 [86] Promotes mtp53 degradation [87] PIRH2 Induces ubiquitination and degradation of wtp53 [88] Promotes mtp53 degradation [89] COP1 Induces ubiquitination and degradation of wtp53 [90] Promotes mtp53 degradation [91] TRIM protei…”
BackgroundMethodTrim24 prompts tumor progression via inducing EMT in renal cell carcinoma
Jiang, T., Mao, H., Chen, Q., Linsheng, C., He, Y., Gao, X., Chen, W., & Zhang, H. (2020) · Open Medicine · doi:10.1515/med-2020-0206 · Cited by 15
Shi, L., Huang, C., Luo, Q., Xia, Y., Liu, H., Li, L., Liu, W., Ma, W., Fang, J. S., Tang, L., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.22348 · Cited by 14
Chi, J., Yang, Q. H., Xie, X.-F., Yang, X.-Z., Zhang, M.-Y., Wang, H., & Xu, G.-L. (2016) · Aging · doi:10.18632/aging.101037 · Cited by 14
“As a member of the tripartite motif (TRIM) protein family, which is defined as E3 ubiquitin ligases, TRIM24 can ubiquitylate and negatively regulates the level of p53 [8, 9].”
Wang, J., Liang, X., Yu, T., Xu, Y., Xu, L., Zhang, X., Ma, J., Wang, Y., & He, S. (2018) · Cell Biology International · doi:10.1002/cbin.11035 · Cited by 14
“Evidence suggests that mutation of TRIM24 in drosophila results in apoptosis, which can be rescued by p53-depletion (Allton et al., 2009).”
BackgroundRegulation of Apoptosis During Porcine Circovirus Type 2 Infection
Pan, Y., Li, P., Jia, R., Wang, M., Yin, Z., & Cheng, A. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.02086 · Cited by 15
Wang, Y., Yao, Y., Liu, Z., Long, S., Feng, Y., Fang, Q. Z., Wu, D., Zhu, Q., Zai, H., Xiao, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63685-8 · Cited by 14
“This difference could be attributed to the pivotal role of Wnt/β-catenin signaling in the initiation and progression of CRC. Correspondingly, we discussed these results together with previous related studies in the revised manuscript (Discussion section, lines 257-260).”
Huang, Y., Gao, Y., Lin, Z., & Miao, H. (2024) · Genes & Diseases · doi:10.1016/j.gendis.2024.101240 · Cited by 14
TRIM24 Expression as an Independent Biomarker for Prognosis and Tumor Recurrence in HNSCC
Klapper, L., Idel, C., Kuppler, P., Jagomast, T., von Bernuth, A., Bruchhage, K., Rades, D., Offermann, A., Kirfel, J., Perner, S., et al. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12060991 · Cited by 13
Tardi, N. J., Cook, M. E., & Edwards, K. A. (2012) · Fly · doi:10.4161/fly.20525 · Cited by 13
Development of small molecule inhibitors of BRPF1 and TRIM24 bromodomains
Palmer, W. S. (2016) · Drug Discovery Today Technologies · doi:10.1016/j.ddtec.2016.06.005 · Cited by 13
“Diverse functions have been attributed to TRIM24, which include acting as an E3-ubiquitin ligase of p53 thereby promoting its degradation [15,16], functioning as a coactivator of the estrogen receptor [14], as well as interacting with the retinoic acid receptor and repressing its transcriptional activity [17].”
BackgroundRegulation of Epithelial–Mesenchymal Plasticity by the E3 Ubiquitin-Ligases in Cancer
Rodríguez-Alonso, A., Casas-Pais, A., Roca‐Lema, D., Graña, B., Romay, G., & Figueroa, A. (2020) · Cancers · doi:10.3390/cancers12113093 · Cited by 13
Inducible Protein Traps with Dominant Phenotypes for Functional Analysis of theDrosophilaGenome
Singari, S., Javeed, N., Tardi, N. J., Marada, S., Carlson, J. C., Kirk, S., Thorn, J. M., & Edwards, K. A. (2013) · Genetics · doi:10.1534/genetics.113.157529 · Cited by 13
“…striking, such as the ability of klu to fuse the head to the thorax under pnr-GAL4 control (Figure S5), and the ability of bon, a regulator of p53 and nuclear receptors (Beckstead et al. 2001, 2005; Allton et al. 2009), to drive production of hairs on the retina (see SEM data in Tardi et al. 2012).”
BackgroundImpact of Adenovirus E4-ORF3 Oligomerization and Protein Localization on Cellular Gene Expression
Vink, E. I., Zheng, Y., Yeasmin, R., Stamminger, T., Krug, L. T., & Hearing, P. (2015) · Viruses · doi:10.3390/v7052428 · Cited by 13
“p53 and Smad4 for ubiquitin-dependent proteasome degradation [33,34].”
BackgroundCytoplasmic Protein Serine/Threonine Kinases
Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_5 · Cited by 11
Novel insights into the recognition of acetylated histone H4 tail by the TRIM24 PHD-Bromo module
Bardhan, I., Barman, S., Roy, A., & Sudhamalla, B. (2023) · Biochemical Journal · doi:10.1042/bcj20230011 · Cited by 12
Li, C., Xin, H., Shi, Y., & Mu, J. (2020) · Human & Experimental Toxicology · doi:10.1177/0960327120938845 · Cited by 12
“TRIM24 is a RING-type E3 ubiquitin ligase domaincontaining protein that can polyubiquitinate p53 and promote its degradation.(8) Interestingly, studies have suggested that TRIM24 is a crucial cancer-related protein that is dysregulated in a wide range of human cancer types.”
BackgroundVink, E. I., Yondola, M. A., Wu, K., & Hearing, P. (2011) · Virology · doi:10.1016/j.virol.2011.10.033 · Cited by 15
“Furthermore, TIF1α has been shown to promote p53 ubiquitination, leading to its proteosome-dependent degradation (Allton et al., 2009).”
BackgroundGuo, Y., Hu, G. M., Tian, B., Ma, M., Long, F., & Chen, M. (2022) · Cancers · doi:10.3390/cancers14246218 · Cited by 11
“In addition, TRIM24 has been identified as an interacting partner of p53, and it is implicated in the ubiquitin-dependent degradation of p53 [19].”
BackgroundHirose, Y., Sato, S., Hashiya, K., Bando, T., & Sugiyama, H. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00613 · Cited by 11
Xu, C., Chen, G., Yu, B., Sun, B., Zhang, Y., Zhang, M., Yang, Y., Xiao, Y., Cheng, S., Li, Y., et al. (2024) · Advanced Science · doi:10.1002/advs.202400023 · Cited by 13
Dermatomyositis: Myositis‐specific autoantibodies and skin manifestations
Fujimoto, M. (2012) · Clinical and Experimental Neuroimmunology · doi:10.1111/j.1759-1961.2012.00028.x · Cited by 11
Ursodeoxycholic acid modulates the ubiquitin-proteasome degradation pathway of p53
Amaral, J. D., Castro, R. E., Solá, S., Steer, C. J., & Rodrigues, C. M. P. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.121 · Cited by 12
The Association between TIF1 Family Members and Cancer Stemness in Solid Tumors
Czerwińska, P., Wlodarczyk, N. A., Jaworska, A. M., & Mackiewicz, A. A. (2021) · Cancers · doi:10.3390/cancers13071528 · Cited by 11
Biswas, S., Killick, E., Jochemsen, A. G., & Lunec, J. (2014) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2014.892924 · Cited by 11
“, phosphorylation) of p53, which affects its transcriptional activity [39,40]; ii) Tissue-specific expression and activity of non-HDM p53-binding E3 ubiquitin ligases, which could modulate responses to p53-RA drugs in a HDM2-independent manner [41,42]; iii) Tissue-specific differences in the binding affinities of reac…”
BackgroundThiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_2 · Cited by 9
Pichlak, M., Sobierajski, T., Błażewska, K. M., & Gendaszewska‐Darmach, E. (2023) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2023.2254012 · Cited by 10
“An approach to restoring p53 functions and causing tumour cells to undergo induced apoptosis may be provided by therapeutic targeting of the TRIM24 protein 123 .”
Emerging roles of tripartite motif family proteins ( TRIMs ) in breast cancer
Cao, J., Yang, M., Guo, D., Tao, Z., & Hu, X. (2024) · Cancer Medicine · doi:10.1002/cam4.7472 · Cited by 9
“212 Pathiraja et al observed that ectopic expression of TRIM24 in immortalized HMECs (TRIM24 iHMECs) would activate aerobic glycolysis as well as greatly increase glucose metabolism, and functionally promote the malignant biological behavior of BC. 213 TRIM58, 217 and TRIM62 169 are expressed at low levels in BC sampl…”
BackgroundInfluentialBouvier, C., Gonzalez-Santamarta, M., Profitós-Pelejà, N., Armengol, M., Quinet, G., Alasseur, Q., Ceccato, L., Xolalpa, W., Freire, R., Guillermet‐Guibert, J., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02355-6 · Cited by 10
“The absence of mycoplasma was routinely checked in all cultures by PCR and the identity of all cell lines was veri fi ed by using AmpFISTR identi fi er kit (Thermo Fisher).”
Double vulnerability of active-NRF2 lung squamous cell carcinoma to NRF2 and TRIM24
Sánchez-Ortega, M., Garrido, A., Sanz, L., Torres‐Pérez, R., Hernandez, C., Gutiérrez-Uzquiza, Á., Tsao, M., & Carrera, A. C. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02401-y · Cited by 10
“TRIM24 functions as an E3-ubiquitin ligase for p53, as a coactivator of the estrogen receptor and as repressor of retinoic acid receptor transcriptional activity [18].”
Lai, M., Liu, M., Li, D., Zhang, R., Wang, L., Li, X., Chen, S., Wu, S., Xiao, S., Wei, L., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107818 · Cited by 10
Tumor Metabolism: MAGE-A Proteins Help TRIM Turn Over AMPK
Shaw, R. J. (2015) · Current Biology · doi:10.1016/j.cub.2015.03.019 · Cited by 10
Hippo pathway and Bonus control developmental cell fate decisions in the Drosophila eye
Zhao, H., Moberg, K. H., & Veraksa, A. N. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.02.005 · Cited by 7
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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