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Coping with stress: multiple ways to activate p53
Abstract
Over the years, p53 has been shown to sit at the centre of an increasingly complex web of incoming stress signals and outgoing effector pathways. The number and diversity of stress signals that lead to p53 activation illustrates the breadth of p53's remit - responding to a wide variety of potentially oncogenic insults to prevent tumour development. Interestingly, different stress signals can use different and independent pathways to activate p53, and there is some evidence that different stress signals can mediate different responses. How each of the responses to p53 contributes to inhibition of malignant progression is beginning to be clarified, with the hope that identification of responses that are key to tumour suppression will allow a more focused and effective search for new therapeutic targets. In this review, we will highlight some recently identified roles for p53 in tumour suppression, and discuss some of the numerous mechanisms through which p53 can be regulated and activated.
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“p53 is activated in response to stress signals—DNA damage, oncogene activation, ribosomal stress and hypoxia4 —and leads to growth suppression by inducing cell cycle arrest or cell death.”
From Census and evaluation of p53 target genes (2017) · cites this paper as [4]
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RETRACTED: The E3 SUMO Ligase PIASy Is a Regulator of Cellular Senescence and Apoptosis
Bischof, O., Schwamborn, K., Martin, N., Werner, A., Sustmann, C., Grosschedl, R., & Dejean, A. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.016 · Cited by 172
RetractedVogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“The p53 protein is a transcription factor that regulates the expression of a large number of target genes (Vogelstein et al., 2000).”
BackgroundCDK inhibitors: positive and negative regulators of G1-phase progression
Sherr, C. J., & Roberts, J. M. (1999) · Genes & Development · doi:10.1101/gad.13.12.1501 · Cited by 6,115
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649
Germ Line p53 Mutations in a Familial Syndrome of Breast Cancer, Sarcomas, and Other Neoplasms
Malkin, D., Li, F. P., Strong, L. C., Fraumeni, J. F., Nelson, C. E., Kim, D. H., Kassel, J., Gryka, M. A., Bischoff, F. Z., Tainsky, M. A., et al. (1990) · Science · doi:10.1126/science.1978757 · Cited by 3,765
DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
Bartkova, J., Hořejší, Z., Koed, K., Krämer, A., Tort, F., Zieger, K., Guldberg, P., Sehested, M., Nesland, J. M., Lukas, C., et al. (2005) · Nature · doi:10.1038/nature03482 · Cited by 2,688
PUMA, a Novel Proapoptotic Gene, Is Induced by p53
Nakano, K., & Vousden, K. H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00214-3 · Cited by 2,315
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Items 101–200 of 524
Min, M., & Spencer, S. L. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000178 · Cited by 85
Mitochondrial dynamics regulating chemoresistance in gynecological cancers
Kong, B., Tsuyoshi, H., Orisaka, M., Shieh, D., Yoshida, Y., & Tsang, B. K. (2015) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12883 · Cited by 80
Molecular Mechanisms of Anticancer Activities of Puerarin
Ahmad, B., Khan, S., Liu, Y., Xue, M., Nabi, G., Kumar, S., Alshwmi, M., & Qarluq, A. W. (2020) · Cancer Management and Research · doi:10.2147/cmar.s233567 · Cited by 76
Application of Multifunctional Nanomaterials in Radioprotection of Healthy Tissues
Xie, J., Wang, C., Zhao, F., Gu, Z., & Zhao, Y. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201800421 · Cited by 77
Hypoxia-Induced Modulation of Apoptosis and BCL-2 Family Proteins in Different Cancer Cell Types
Sermeus, A., Genin, M., Maincent, A., Fransolet, M., Notte, A., Leclère, L., Riquier, H., Arnould, T., & Michiels, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047519 · Cited by 77
Autophagy regulation in cancer development and therapy.
White, E. J., Martín, V., Liu, J.-L., Klein, S. R., Piya, S., Gomez‐Manzano, C., Fueyo-Margareto, J., & Jiang, H. (2011) · Europe PMC (PubMed Central) · Cited by 76
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Martinez-Rivera, M., & Siddik, Z. H. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.12.026 · Cited by 80
Hasegawa, H., Yamada, Y., Iha, H., Tsukasaki, K., Nagai, K., Atogami, S., Sugahara, K., Tsuruda, K., Ishizaki, A., & Kamihira, S. (2009) · Leukemia · doi:10.1038/leu.2009.171 · Cited by 75
Becker, J. C., Schrama, D., & Houben, R. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8483-6 · Cited by 73
Merkel cell carcinoma: molecular pathogenesis, clinical features and therapy
Becker, J. C., Kauczok, C. S., Ugurel, S., Eib, S., Bröcker, E., & Houben, R. (2008) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1111/j.1610-0387.2008.06830.x · Cited by 70
USP4 inhibits p53 and NF-κB through deubiquitinating and stabilizing HDAC2
Li, Z., Hao, Q., Luo, J., Xiong, J., Zhang, S., Wang, W., Bai, L., Wang, W., Chen, M., Wang, W., et al. (2015) · Oncogene · doi:10.1038/onc.2015.349 · Cited by 73
Regulation of the Mdm2–p53 pathway by the ubiquitin E3 ligase MARCH7
Zhao, K., Yang, Y., Zhang, G., Wang, C., Wang, D., Wu, M., & Mei, Y. (2018) · EMBO Reports · doi:10.15252/embr.201744465 · Cited by 70
Regulation of p53 by TopBP1: a Potential Mechanism for p53 Inactivation in Cancer
Liu, K., Bellam, N., Lin, H., Wang, B., Stockard, C. R., Grizzle, W. E., & Lin, W.-C. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01140-08 · Cited by 70
Chen, R., Cui, Y., Zhang, X., Zhang, Y., Chen, M., Zhou, T., Lan, X., Dong, W., & Pan, C. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03407 · Cited by 73
Turrell, F. K., Kerr, E. M., Gao, M., Thorpe, H., Doherty, G. J., Cridge, J., Shorthouse, D., Speed, A., Samarajiwa, S., Hall, B. A., et al. (2017) · Genes & Development · doi:10.1101/gad.298463.117 · Cited by 71
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de Beco, S., Ziosi, M., & Johnston, L. A. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23783 · Cited by 70
Potapova, T., Seidel, C. W., Box, A., Rancati, G. I., & Li, R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0268 · Cited by 68
Zhang, Y., Huang, Y., Li, Z., Wu, H., Zou, B., & Xu, Y. H. (2023) · Cancers · doi:10.3390/cancers15143585 · Cited by 70
Pereboom, T. C., van Weele, L. J., Bondt, A., & MacInnes, A. W. (2011) · Blood · doi:10.1182/blood-2011-04-351460 · Cited by 69
Hung, J., Chen, C.-Y., Omar, H. A., Huang, K., Tsao, C.-C., Chiu, C., Chen, Y., Chen, P., & Teng, Y. (2015) · Environmental Toxicology · doi:10.1002/tox.22190 · Cited by 70
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Collina, S. (2014) · Medicinal Chemistry · doi:10.4172/2161-0444.s1-004 · Cited by 70
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Chow, A., Hao, Y., & Yang, X. (2009) · International Journal of Cancer · doi:10.1002/ijc.24878 · Cited by 72
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Chillón, I., & Pyle, A. M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw599 · Cited by 67
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DeBardeleben, H. K., Lopes, L. E., Nessel, M. P., & Raizen, D. M. (2017) · Genetics · doi:10.1534/genetics.117.300070 · Cited by 65
Ohbayashi, I., Lin, C.-Y., Shinohara, N., Matsumura, Y., Machida, Y., Horiguchi, G., Tsukaya, H., & Sugiyama, M. (2017) · The Plant Cell · doi:10.1105/tpc.17.00255 · Cited by 63
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Hao, X., Han, F., Zhang, N., Chen, H., JIANG, X. H., Yin, L., Liu, W., Wang, D., Chen, J., Cui, Z.-H., et al. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0202-8 · Cited by 61
Friedman, J., Nottingham, L. K., Duggal, P., Pernas, F. G., Yan, B., Yang, X. P., Chen, Z., & Waes, C. V. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1591 · Cited by 59
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Altman, B. J., & Dang, C. V. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08651.x · Cited by 66
Ahuja, D., Goyal, A., & Ray, P. S. (2016) · RNA Biology · doi:10.1080/15476286.2016.1229734 · Cited by 62
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Guo, Z., Hu, G., Wang, H., Li, Z., & Liu, N. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.12.136 · Cited by 64
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Liu, S., Kim, T.-H., Franklin, D. A., & Zhang, Y. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.086 · Cited by 57
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Navalkar, A., Ghosh, S., Pandey, S., Paul, A., Datta, D., & Maji, S. K. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00796 · Cited by 56
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Birts, C. N., Banerjee, A., Darley, M., Dunlop, C. R., Nelson, S., Nijjar, S. K., Parker, R., West, J. J., Tavassoli, A., Rose-Zerilli, M. J. J., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aau9529 · Cited by 56
Shaked, H., Shiff, I., Kott-Gutkowski, M., Siegfried, Z., Haupt, Y., & Simon, I. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0865 · Cited by 57
Weiss, M. B., Vitolo, M. I., Mohseni, M., Rosen, D. M., Denmeade, S. R., Park, B. H., Weber, D. J., & Bachman, K. E. (2010) · Oncogene · doi:10.1038/onc.2010.220 · Cited by 54
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Luo, J., Lu, Z., Lu, X., Chen, L., Cao, J., Zhang, S., Yang, L., & Zhou, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077682 · Cited by 56
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Koeppel, M., van Heeringen, S. J., Smeenk, L., Navis, A. C., Janssen‐Megens, E. M., & Lohrum, M. A. E. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn940 · Cited by 57
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Seiwert, N., Neitzel, C., Stroh, S., Frisan, T., Audebert, M., Toulany, M., Kaina, B., & Fahrer, J. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.418 · Cited by 54
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Chen, Z., Zhao, S., Liu, Y., Yang, P., Ai, Q., Zhang, W., Xu, W., Zhang, Y., Zhang, Y., & Mai, K. (2018) · Aquaculture Research · doi:10.1111/are.13847 · Cited by 49
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Guha, A., Ahuja, D., Mandal, S. D., Parasar, B., Deyasi, K., Roy, D., Sharma, V., Willard, B. B., Ghosh, A., & Ray, P. S. (2019) · iScience · doi:10.1016/j.isci.2019.05.002 · Cited by 47
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Allison, S. J., Bryk, J., Clemett, C. J., Faulkner, R. A., Ginger, M. L., Griffiths, H. B. S., Harmer, J., Owen‐Lynch, P. J., Pinder, E., Wurdak, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23983-3 · Cited by 42
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Hu, D. G., Rogers, A., & Mackenzie, P. I. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.091603 · Cited by 42
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Paridaen, J. T. M. L., Janson, E., Utami, K. H., Pereboom, T. C., Essers, P., van Rooijen, C., Živković, D., & MacInnes, A. W. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.04.028 · Cited by 42
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Zhu, L., Huang, S., Li, J., Chen, J., Yao, Y., Li, L., Guo, H., Xiang, X., Deng, J., & Xiong, J. (2020) · Gene · doi:10.1016/j.gene.2020.144556 · Cited by 40
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Metadata
- Authors
- Horn, H. F., & Vousden, K. H.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Corresponding author
- Vousden, K H
- Venue
- Oncogene
- Published
- 2007-02-26
- Volume
- 26
- Issue
- 9
- Pages
- 1306-1316
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W2035188342
- Semantic Scholar
- ea46e0441d9175c80c0ddbd29c6fc13c60a82939
- Cited by
- 522
- References
- 167
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 18 · 2023: 22 · 2022: 20 · 2021: 30 · 2020: 23 · 2019: 27 · 2018: 35 · 2017: 37 · 2016: 35 · 2015: 30 · 2014: 26 · 2013: 36 · 2012: 26
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- p53, stress signals, p53 activation, tumor suppression, stress response pathways, malignant progression, therapeutic target
- MeSH terms
- Humans, Neoplasms, Signal Transduction, Tumor Suppressor Protein p53, Oxidative Stress
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