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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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Nucleosome assembly proteins NAP1L1 and NAP1L4 modulate p53 acetylation to regulate cell fate
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Roles of Polo-like kinase 3 in suppressing tumor angiogenesis
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Gambichler, T., Kammann, S., Tigges, C., Kobus, S., Skrygan, M., Meier, J. J., Köhler, C. U., Scola, N., Stücker, M., Bechara, F. G., et al. (2011) · Regulatory Peptides · doi:10.1016/j.regpep.2011.02.003 · Cited by 24
p53 Is a Host Cell Regulator during Herpes Simplex Encephalitis
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RetractedFunctional relationship between p53 and RUNX proteins
Bae, S., Kolinjivadi, A. M., & Ito, Y. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy076 · Cited by 22
Wu, M., Sun, Y., Xu, F., Liang, Y., Liu, H., & Yi, Y. (2019) · Journal of Cancer · doi:10.7150/jca.29440 · Cited by 22
Apak competes with p53 for direct binding to intron 1 of p53AIP1 to regulate apoptosis
Yuan, L., Tian, C., Wang, H., Song, S., Li, D., Xing, G., Yin, Y., He, F., & Zhang, L. (2012) · EMBO Reports · doi:10.1038/embor.2012.10 · Cited by 22
Song, J., Lee, B., Kang, S., Oh, Y., Kim, E., Kim, C. H., Song, H., & Lee, J. E. (2016) · Experimental Neurobiology · doi:10.5607/en.2016.25.1.24 · Cited by 22
“The activation of p53 has been reported that it could promote cell cycle arrest and DNA repair [7].”
BackgroundProtein phosphatase 5 and the tumor suppressor p53 down-regulate each other's activities in mice
Wang, J., Shen, T., Zhu, W., Dou, L., Gu, H., Zhang, L., Yang, Z., Chen, H., Zhou, Q., Sánchez, E. R., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004256 · Cited by 22
“regulation of p53 phosphorylation is a highly complex event and may require other posttranslational modifications to achieve significant changes in biological activity (22).”
BackgroundDecoding the dual role of autophagy in cancer through transcriptional and epigenetic regulation
Yu, Y. S., Kim, I. S., & Baek, S. H. (2025) · FEBS Letters · doi:10.1002/1873-3468.70060 · Cited by 24
“The tumor suppressor p53 is a central regulator of cellular homeostasis and is involved in the regulation of cellular processes, including DNA repair, cell cycle arrest, cellular senescence, apoptosis, and autophagy [72].”
Zhuang, J., Kamp, W. M., Li, J., Liu, C., Kang, J., Wang, P., & Hwang, P. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.745737 · Cited by 22
Ding, L. J., Sun, R., & Zhang, X. (2017) · Oncotarget · doi:10.18632/oncotarget.15508 · Cited by 21
Regulation of Tip60‐dependent p53 acetylation in cell fate decision
Wang, P., Bao, H., Zhang, X., Liu, F., & Wang, W. (2018) · FEBS Letters · doi:10.1002/1873-3468.13287 · Cited by 21
Post-translational and transcriptional dynamics – regulating extracellular vesicle biology
Claridge, B., Kastaniegaard, K., Stensballe, A., & Greening, D. W. (2018) · Expert Review of Proteomics · doi:10.1080/14789450.2019.1551135 · Cited by 21
Anticancer Drug-Induced Epithelial-Mesenchymal Transition via p53/miR-34a axis in A549/ABCA3 Cells
Yamamoto, A., Kawami, M., Konaka, T., Takenaka, S., Yumoto, R., & Takano, M. (2019) · Journal of Pharmacy & Pharmaceutical Sciences · doi:10.18433/jpps30660 · Cited by 21
A CD24‐p53 axis contributes to African American prostate cancer disparities
Liu, W., Zhang, Y., Wei, S., Bae, S., Yang, W., Smith, G. J., Mohler, J. L., Fontham, E. T. H., Bensen, J. T., Sonpavde, G., et al. (2020) · The Prostate · doi:10.1002/pros.23973 · Cited by 21
The Ins and Outs of HOPS/TMUB1 in biology and pathology
Fazia, M. A. D., Castelli, M., Piobbico, D., Pieroni, S., & Servillo, G. (2020) · FEBS Journal · doi:10.1111/febs.15539 · Cited by 21
Shimizu, S., Sunagawa, Y., Hajika, N., Natsumi, Y., Katanasaka, Y., Funamoto, M., Miyazaki, Y., Sari, N., Shimizu, K., Hasegawa, K., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.65664 · Cited by 21
Busbee, P. B., Bam, M., Yang, X., Abdulla, O. A., Zhou, J., Ginsberg, J. P., Aiello, A. E., Uddin, M., Nagarkatti, M., & Nagarkatti, P. S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2021.815840 · Cited by 24
“In response to DNA damage or some abnormal oncogene activation, TP53 will act as a tumor suppressor by preventing tumor growth and development through several pathways including apoptosis, senescence, and cell cycle arrest (53).”
BackgroundZhang, L., Hou, N., Chen, B., Kan, C., Han, F., Zhang, J., & Sun, X. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.908772 · Cited by 21
“Acetylation increases the stability of p53 and is essential for its ability to repair DNA damage (Kruse and Gu, 2009).”
BackgroundPinto, E. M., Ribeiro, R. C., Kletter, G. B., Lawrence, J. P., Jenkins, J. J., Wang, J., Shurtleff, S. A., McGregor, L. M., Kriwacki, R. W., & Zambetti, G. P. (2010) · Familial Cancer · doi:10.1007/s10689-010-9392-z · Cited by 21
“The C-terminal regulatory domain of TP53 is intrinsically disordered [6], has post-translational modification at numerous sites, and interacts with numerous signaling partners [ 7 ].”
BackgroundZajkowicz, A., & Rusin, M. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.09.002 · Cited by 21
Squaring up to DNA: pentapeptide repeat proteins and DNA mimicry
Shah, S. S., & Heddle, J. G. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6151-3 · Cited by 21
“Further details can be found in recent reviews (Putnam et al. 1999; Wang et al. 2014a) including details of S. Shah : J. G. Heddle (*) Heddle Initiative Research Unit, RIKEN, 2-1, Hirosawa, Wako, Saitama 351-0198, Japan e-mail: heddle@riken.jp S. Shah Department of Life Science and Medical Bioscience, Waseda Universit…”
BackgroundLessons from interconnected ubiquitylation and acetylation of p53: think metastable networks
Benkirane, M., Sardet, C., & Coux, O. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380098 · Cited by 24
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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