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Modes of p53 regulation.
Open accessAbstract
The traditional view of p53 activation includes three steps-p53 stabilization, DNA binding, and transcriptional activation. However, recent studies indicate that each step of p53 activation is more complex than originally anticipated. Moreover, both genetic studies in mice and in vitro studies with purified components suggest that the classical model may not be sufficient to explain all aspects of p53 activation in vivo. To reconcile these differences, we propose that antirepression, the release of p53 from repression by factors such as Mdm2 and MdmX, is a key step in the physiological activation of p53.
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“Activation of p53 is dependent on various post translational modifications such as phosphorylation, methylation, acetylation, sumoylation, ubiquitination, and neddylation (Kruse and Gu, 2009).”
From Mechanisms of Cellular Senescence: Cell Cycle Arrest and Senescence Associated Secretory Phenotype (2021) · cites this paper as Kruse and Gu, 2009
In the citing paper
“This transcriptional antagonism can take place within the nucleus, as Mdm2 and Mdmx have been detected at p53-responsive promoter elements in chromatin [2].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [2]
In the citing paper
“MDM2 is a known E3 ubiquitin ligase that acts as a powerful inhibitor of the tumor suppressor P53 [141].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [141]
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Citations
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Dose-Response Modeling of Etoposide-Induced DNA Damage Response
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“Although there are many potential modifications of p53 that are associated with specific p53 functions, serine 15 phosphorylation represents an early event that is vital for nuclear localization and is often used as a marker of p53 activation (Kruse and Gu, 2009; Rashi-Elkeles et al., 2011).”
BackgroundLv, X., Cai, Z., & Su, L. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3692 · Cited by 27
“If the cell repair cannot be completed, the cell tends to undergo apoptosis mediated by TP53 protein (10).”
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USP3 stabilizes p53 protein through its deubiquitinase activity
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“Ser-15 phosphorylation of p53 is known to be catalyzed by apical DDR kinases, such as ATM, following DNA damage [33,63].”
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MDMX exerts its oncogenic activity via suppression of retinoblastoma protein
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ATM Suppresses SATB1-Induced Malignant Progression in Breast Epithelial Cells
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Resveratrol induces cell cycle arrest and apoptosis in human eosinophils from asthmatic individuals
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“Previous studies have indicated that p53 serves an important role in determining the response of cells to different types and levels of stressful stimuli, and regulates downstream cell cycle, cell metabolism, DNA repair and apoptotic signaling pathways (23-25).”
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“Because the tumor suppressor p53, which is phosphorylated at Ser18 (corresponding to Ser15 of human p53) by ataxia telangiectasia mutated (ATM) protein in response to DNA damage [18], might play a critical role in apoptosis induction, we examined the levels of phosphorylated p53 (p-p53) and p53.”
BackgroundGlobal analysis of mutual interaction surfaces of nucleosomes with comprehensive point mutants
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“Highly conserved proteins often have multiple functional and structural domains and motifs (Hoffmann et al. 1990; Kruse & Gu 2009).”
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“However, a possible favorable interaction between HDACi and MDM2 inhibitors has not yet been studied, although this combination appears to be especially attractive, because the acetylation of p53 critically contributes to its activation [ 15 ]—in fact, acetylation has been found to be essential for p53-mediated apopto…”
BackgroundThe p53 network as therapeutic target in gastroenteropancreatic neuroendocrine neoplasms
Briest, F., & Grabowski, P. (2015) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2015.03.006 · Cited by 26
“Depending on the sensor, the state of the cell cycle and the intensity of the stimulus, p53 is activated and stabilized versus MDM2 (murine double minute 2) mainly by ATM/ATR (Ataxia telangiectasia mutated, Ataxia telangiectasia and Rad3-related protein), CHK2 (checkpoint kinase 2), DNA-PK (DNA-dependent protein kinas…”
BackgroundAtomic Structure of Dual-Specificity Phosphatase 26, a Novel p53 Phosphatase
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Efficient Reactivation of p53 in Cancer Cells by a Dual MdmX/Mdm2 Inhibitor
Qin, L., Yang, F., Zhou, C. K., Chen, Y., Zhang, H., & Su, Z. (2014) · Journal of the American Chemical Society · doi:10.1021/ja509223m · Cited by 26
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The Biological Significance of Zinc in Inflammation and Aging
Bao, B., Ahmad, A., Azmi, A. S., Li, Y., Prasad, A. S., & Sarkar, F. H. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397803-5.00002-2 · Cited by 26
The DNA repair complex Ku70/86 modulates Apaf1 expression upon DNA damage
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“In particular, after DNA damage induction, Ku70 and Ku86 form the huge DNA-PK complex with the DNA-PKcs, which in turn activates several pathways by the direct or indirect phosphorylation of different substrates, such as p53.(36) In this scenario, the upregulation of Apaf1 could be the result of both the Ku displaceme…”
BackgroundAutophagy as the effector and player in DNA damage response of cells to genotoxicants
Zhang, S.-M., Shang, Z., & Zhou, P. (2015) · Toxicology Research · doi:10.1039/c5tx00043b · Cited by 23
Tumor Suppressor RASSF1A Promoter: p53 Binding and Methylation
Tian, Y., Hou, Y., Zhou, X., Cheng, H., & Zhou, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017017 · Cited by 25
Pal, D., Mukhopadhyay, D., Ramaiah, M. J., Sarma, P. N., Bhadra, U., & Bhadra, M. P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159092 · Cited by 25
The role of acetylation sites in the regulation of p53 activity
Wang, Y., Chen, Y., Chen, Q., Zhang, X., Wang, H., Wang, Z., Wang, J., & Tian, C. (2019) · Molecular Biology Reports · doi:10.1007/s11033-019-05141-7 · Cited by 27
Metadata
- Authors
- Kruse, J.-P., & Gu, W.
- Affiliations
- Columbia University (US)
- Corresponding author
- Gu, Wei
- ORCID
- Gu, Wei
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 137
- Issue
- 4
- Pages
- 609-622
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3737742
- OpenAlex
- W2025722611
- Cited by
- 1,610
- References
- 152
- Citations by year
- 2026: 31 · 2025: 49 · 2024: 52 · 2023: 57 · 2022: 81 · 2021: 98 · 2020: 75 · 2019: 73 · 2018: 100 · 2017: 98 · 2016: 102 · 2015: 108 · 2014: 142 · 2013: 127 · 2012: 128
- FWCI
- 12.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (2r01ca085533-16)
- National Cancer Institute (R01-CA085533, R01CA131439, P01CA097403, R01CA104843, P01CA080058, R01CA098821, R01CA129627)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- p53 activation, p53 regulation, MDM2, MDMX, p53 stabilization, DNA binding, transcriptional activation, tumor suppressor
- MeSH terms
- Animals, Humans, Protein Processing, Post-Translational, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Proto-Oncogene Proteins c-mdm2
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