Coping with stress: multiple ways to activate p53

Horn, H F; Vousden, K H

doi:10.1038/sj.onc.1210263

Cited by 524Cancer-related Molecular PathwaysCell death mechanisms and regulationPI3K/AKT/mTOR signaling in cancer

Coping with stress: multiple ways to activate p53

Horn, H F, Vousden, K H·2007·Oncogene

DOI 10.1038/sj.onc.1210263

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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 including DNA damage, oncogene activation, ribosomal stress and hypoxia.
“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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Boyd, S. D., Tsai, K. Y., & Jacks, T. (2000) · Nature Cell Biology · doi:10.1038/35023500 · Cited by 334 · see citing works
MDM2 interacts with MDMX through their RING finger domains
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The PTEN/MMAC1/TEP tumor suppressor gene decreases cell growth and induces apoptosis and anoikis in breast cancer cells
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Small molecule inhibitors of HDM2 ubiquitin ligase activity stabilize and activate p53 in cells
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Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1
Asher, G., Lotem, J., Cohen, B., Sachs, L., & Shaul, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.1188 · Cited by 317 · see citing works
TRB3 Links the E3 Ubiquitin Ligase COP1 to Lipid Metabolism
Qi, L., Heredia, J. E., Altarejos, J. Y., Screaton, R. A., Goebel, N., Niessen, S., MacLeod, I., Liew, C. W., Kulkarni, R., Bain, J. R., et al. (2006) · Science · doi:10.1126/science.1123374 · Cited by 311 · see citing works
Damage-mediated Phosphorylation of Human p53 Threonine 18 through a Cascade Mediated by a Casein 1-like Kinase
Sakaguchi, K., Saito, S., Higashimoto, Y., Roy, S., Anderson, C. W., & Appella, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.13.9278 · Cited by 293 · see citing works
Tumour incidence, spectrum and ploidy in mice with a large deletion in the p53 gene.
Purdie, C. A., Harrison, D. J., Peter, A., Dobbie, L., White, S., Howie, S., Salter, D. M., Bird, C., Wyllie, A. H., & Hooper, M. L. (1994) · PubMed · Cited by 290 · see citing works
Stabilization of the MDM2 Oncoprotein by Interaction with the Structurally Related MDMX Protein
Sharp, D. A., Kratowicz, S. A., Sank, M. J., & George, D. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38189 · Cited by 286 · see citing works
Mutual Dependence of MDM2 and MDMX in Their Functional Inactivation of p53
Gu, J., Kawai, H., Nie, L., Kitao, H., Wiederschain, D., Jochemsen, A. G., Parant, J. M., Lozano, G., & Yuan, Z.-M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200150200 · Cited by 265 · see citing works
p300/CBP/p53 interaction and regulation of the p53 response
Grossman, S. R. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02226.x · Cited by 264 · see citing works
Mdm4 and Mdm2 cooperate to inhibit p53 activity in proliferating and quiescent cells <i>in vivo</i>
Francoz, S., Froment, P., Bogaerts, S., De Clercq, S., Maetens, M., Doumont, G., Bellefroid, E., & Marine, J.-C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508476103 · Cited by 260 · see citing works
The Chaperone-associated Ubiquitin Ligase CHIP Is Able to Target p53 for Proteasomal Degradation
Esser, C., Scheffner, M., & Höhfeld, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501574200 · Cited by 260 · see citing works
Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2.
Meulmeester, E., Maurice, M. M., Boutell, C., Teunisse, A. F. A. S., Ovaa, H., Abraham, T. E., Dirks, R. W., & Jochemsen, A. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.024 · Cited by 260 · see citing works
Genetic Inactivation of the Transcription Factor TIF-IA Leads to Nucleolar Disruption, Cell Cycle Arrest, and p53-Mediated Apoptosis
Yuan, X., Zhou, Y., Casanova, E., Chai, M., Kiss, É., Gröne, H., Schütz, G., & Grummt, I. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.023 · Cited by 250 · see citing works
Essential role of ribosomal protein L11 in mediating growth inhibition‐induced p53 activation
Bhat, K., Itahana, K., Jin, A., & Zhang, Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600247 · Cited by 249 · see citing works
MDM2 promotes ubiquitination and degradation of MDMX
Pan, Y., & Chen, J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.15.5113-5121.2003 · Cited by 246 · cited 14× · see citing works
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
BackgroundInfluential
p53 in recombination and repair
Gatz, S. A., & Wiesmüller, L. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401903 · Cited by 242 · see citing works
p53 and Nur77/TR3 – transcription factors that directly target mitochondria for cell death induction
Moll, U. M., Marchenko, N. D., & Zhang, X.-K. (2006) · Oncogene · doi:10.1038/sj.onc.1209601 · Cited by 241 · see citing works
E4F1 Is an Atypical Ubiquitin Ligase that Modulates p53 Effector Functions Independently of Degradation
Cam, L. L., Linares, L. K., Paul, C., Julien, E., Lacroix, M., Hatchi, E., Triboulet, R., Bossis, G., Shmueli, A., Rodríguez, M. S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.09.031 · Cited by 241 · see citing works
p53 Stabilization and Transactivation by a von Hippel-Lindau Protein
Roe, J., Kim, H., Lee, S.-M., Kim, S.-T., Cho, E., & Youn, H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.04.006 · Cited by 240 · see citing works
Critical role for Daxx in regulating Mdm2
Tang, J., Qu, L., Zhang, J., Wang, W., Michaelson, J. S., Degenhardt, Y., El‐Deiry, W. S., & Yang, X. (2006) · Nature Cell Biology · doi:10.1038/ncb1442 · Cited by 239 · see citing works
Polymorphisms in the p53 pathway
Pietsch, E. C., Humbey, O., & Murphy, M. E. (2006) · Oncogene · doi:10.1038/sj.onc.1209367 · Cited by 237 · see citing works
C-Terminal Ubiquitination of p53 Contributes to Nuclear Export
Lohrum, M. A. E., Woods, D. B., Ludwig, R. L., Bálint, É., & Vousden, K. H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8521-8532.2001 · Cited by 237 · see citing works
Self-citation
MDMX overexpression prevents p53 activation by the MDM2 inhibitor Nutlin
Hu, B., Gilkes, D. M., Farooqi, B., Sebti, S. M., & Chen, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600147200 · Cited by 236 · see citing works
Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses
Yoon, K., Nakamura, Y., & Arakawa, H. (2004) · Journal of Human Genetics · doi:10.1007/s10038-003-0122-3 · Cited by 236 · see citing works
Mdmx stabilizes p53 and Mdm2 via two distinct mechanisms
Stad, R., Little, N. A., Xirodimas, D. P., Frenk, R., van der Eb, A. J., Lane, D. P., Saville, M. K., & Jochemsen, A. G. (2001) · The EMBO Reports · doi:10.1093/embo-reports/kve227 · Cited by 234 · see citing works
The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53
Higashitsuji, H., Higashitsuji, H., Itoh, K., Sakurai, T., Nagao, T., Sumitomo, H., Masuda, T., Dawson, S. P., Shimada, Y., Mayer, R. J., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.006 · Cited by 228 · see citing works
MdmX Protects p53 from Mdm2-Mediated Degradation
Jackson, M. W., & Berberich, S. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1001-1007.2000 · Cited by 211 · cited 1× · see citing works
“However, MdmX does not show E3 activity (Jackson and Berberich, 2000; Stad et al., 2001) and functions predominantly by directly inhibiting p53’s transcriptional activity (Shvarts et al., 1996; Francoz et al., 2006).”
Background
MDM2 Promotes Cell Motility and Invasiveness by Regulating E-Cadherin Degradation
Yang, J.-Y., Zong, C. S., Xia, W., Wei, Y., Ali-Seyed, M., Li, Z., Broglio, K., Berry, D. A., & Hung, M.-C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00172-06 · Cited by 211 · see citing works
YY1 inhibits the activation of the p53 tumor suppressor in response to genotoxic stress
Gronroos, E. C., Terentiev, A. A., Punga, T., & Ericsson, J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402283101 · Cited by 210 · see citing works
Tumor suppression and normal aging in mice with constitutively high p53 activity
Mendrysa, S. M., O'Leary, K. A., McElwee, M. K., Michalowski, J., Eisenman, R. N., Powell, D. A., & Perry, M. E. (2006) · Genes & Development · doi:10.1101/gad.1378506 · Cited by 210 · see citing works
The role of p53 in hypoxia-induced apoptosis
Hammond, E. M., & Giaccia, A. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.154 · Cited by 208 · see citing works
FBXO11 Promotes the Neddylation of p53 and Inhibits Its Transcriptional Activity
Abida, W. M., Nikolaev, A. Y., Zhao, W., Zhang, W., & Gu, W. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609001200 · Cited by 201 · see citing works
Degradation of the Tumor Suppressor Smad4 by WW and HECT Domain Ubiquitin Ligases
Morén, A., Imamura, T., Miyazono, K., Heldin, C., & Moustakas, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414027200 · Cited by 200 · see citing works
Topors Functions as an E3 Ubiquitin Ligase with Specific E2 Enzymes and Ubiquitinates p53
Rajendra, R., Malegaonkar, D., Pungaliya, P., Marshall, H., Rasheed, Z. A., Brownell, J. E., Liu, L. F., Lutzker, S. G., Saleem, A., & Rubin, E. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400300200 · Cited by 192 · see citing works
Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3
Patton, J. T., Mayo, L. D., Singhi, A. D., Gudkov, A. V., Stark, G. R., & Jackson, M. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3832 · Cited by 189 · see citing works
HAUSP is Required for p53 Destabilization
Cummins, J. M., & Vogelstein, B. (2004) · Cell Cycle · doi:10.4161/cc.3.6.924 · Cited by 188 · see citing works
Complicating the complexity of p53
Yee, K. S. Y., & Vousden, K. H. (2005) · Carcinogenesis · doi:10.1093/carcin/bgi122 · Cited by 187 · see citing works
Self-citation
Mdmx as an essential regulator of p53 activity
Marine, J., & Jochemsen, A. G. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.151 · Cited by 186 · see citing works
ATM-Mediated Phosphorylations Inhibit Mdmx/Mdm2 Stabilization by HAUSP in Favor of p53 Activation
Meulmeester, E., Pereg, Y., Shiloh, Y., & Jochemsen, A. G. (2005) · Cell Cycle · doi:10.4161/cc.4.9.1981 · Cited by 166 · see citing works
DNA damage-induced MDMX degradation is mediated by MDM2
Kawai, H., Wiederschain, D., Kitao, H., Stuart, J., Tsai, K. K. C., & Yuan, Z.-M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308295200 · Cited by 163 · cited 14× · see citing works
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
BackgroundInfluential
Hdmx modulates the outcome of p53 activation in human tumor cells
Wade, M., Wong, E. T., Tang, M., Stommel, J. M., & Wahl, G. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605405200 · Cited by 163 · see citing works
Synergistic roles of Mdm2 and Mdm4 for p53 inhibition in central nervous system development
Xiong, S., Van Pelt, C. S., Elizondo-Fraire, A. C., Liu, G., & Lozano, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508500103 · Cited by 155 · see citing works
Human Kruppel-like Factor 5 Is a Target of the E3 Ubiquitin Ligase WWP1 for Proteolysis in Epithelial Cells
Chen, C., Sun, X., Guo, P., Dong, X., Sethi, P., Cheng, X., Zhou, J., Ling, J., Simons, J. W., Lingrel, J. B., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506183200 · Cited by 155 · see citing works
Sequence‐specific DNA binding by p53: identification of target sites and lack of binding to p53 ‐ MDM2 complexes.
Zauberman, A., Barak, Y., Ragimov, N., Levy, N., & Oren, M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05941.x · Cited by 151 · see citing works
DAP-kinase induces apoptosis by suppressing integrin activity and disrupting matrix survival signals
Wang, W., Kuo, J., Yao, C. J., & Chen, R. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204050 · Cited by 150 · see citing works
Cancer-Associated Mutations in the MDM2 Zinc Finger Domain Disrupt Ribosomal Protein Interaction and Attenuate MDM2-Induced p53 Degradation
Lindström, M. S., Jin, A., Deisenroth, C., Wolf, G. W., & Zhang, Y. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01307-06 · Cited by 149 · see citing works
Hdmx protein stability is regulated by the ubiquitin ligase activity of Mdm2
de Graaf, P., Little, N. A., Ramos, Y. F. M., Meulmeester, E., Letteboer, S. J. F., & Jochemsen, A. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213034200 · Cited by 143 · cited 1× · see citing works
“…(Sharp et al., 1999; Tanimura et al., 1999), which results in the stabilization of Mdm2 (Stad et al., 2001; Gu et al., 2002) or the Mdm2-mediated degradation of MdmX (de Graaf et al., 2003; Kawai et al., 2003; Pan and Chen, 2003), depending on the relative expression levels of the two proteins.”
Background
MDMX regulation of p53 response to ribosomal stress
Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142 · see citing works
ATM Engages Autodegradation of the E3 Ubiquitin Ligase COP1 After DNA Damage
Dornan, D., Shimizu, H., Mah, A. S., Dudhela, T., Eby, M. T., O’Rourke, K. M., Seshagiri, S., & Dixit, V. M. (2006) · Science · doi:10.1126/science.1127335 · Cited by 141 · see citing works
Regulation of p53 localization and transcription by the HECT domain E3 ligase WWP1
Laine, A., & Ronai, Z. A. (2006) · Oncogene · doi:10.1038/sj.onc.1209924 · Cited by 129 · see citing works
Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth
McDonald, E. R., & El‐Deiry, W. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307459101 · Cited by 121 · see citing works
Mdm2 is involved in the ubiquitination and degradation of G‐protein‐coupled receptor kinase 2
Salcedo, A., Mayor, F., & Penela, P. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601351 · Cited by 119 · see citing works
Loss of the ARF tumor suppressor reverses premature replicative arrest but not radiation hypersensitivity arising from disabled atm function.
Kamijo, T., van de Kamp, E. H., Chong, M. J., Zindy, F., Diehl, J. A., Sherr, C. J., & McKinnon, P. J. (1999) · PubMed · Cited by 117 · see citing works
Gankyrin Is an Ankyrin-repeat Oncoprotein That Interacts with CDK4 Kinase and the S6 ATPase of the 26 S Proteasome
Dawson, S. P., Apcher, S., Mee, M., Mayer, R. J., Higashitsuji, H., Baker, R. T., Uhle, S., Dubiel, W., & Fujita, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m107313200 · Cited by 117 · see citing works
p23, a simple protein with complex activities
Felts, S. J., & Toft, D. O. (2003) · Cell Stress and Chaperones · doi:10.1379/1466-1268(2003)008 · Cited by 116 · see citing works
Policing of oncogene activity by p53
Efeyan, A., Garcı́a-Cao, I., Herranz, D., Velasco-Miguel, S., & Serrano, M. (2006) · Nature · doi:10.1038/443159a · Cited by 114 · see citing works
Savior and slayer: the two faces of p53
Bensaad, K., & Vousden, K. H. (2005) · Nature Medicine · doi:10.1038/nm1205-1278 · Cited by 113 · see citing works
Self-citation
SUMO-1 and p53
Melchior, F., & Hengst, L. (2002) · Cell Cycle · doi:10.4161/cc.1.4.131 · Cited by 109 · see citing works
MAGE-A4 Interacts with the Liver Oncoprotein Gankyrin and Suppresses Its Tumorigenic Activity
Nagao, T., Higashitsuji, H., Nonoguchi, K., Sakurai, T., Dawson, S. P., Mayer, R. J., Itoh, K., & Fujita, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206104200 · Cited by 108 · see citing works
Expression of SUMO-2/3 Induced Senescence through p53- and pRB-mediated Pathways
Li, T., Santockyte, R., Shen, R., Tekle, E., Wang, G., Yang, D. C. H., & Chock, P. B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608236200 · Cited by 107 · see citing works
p53-Independent Activities of MDM2 and Their Relevance to Cancer Therapy
Zhang, Z., & Zhang, R. (2005) · Current Cancer Drug Targets · doi:10.2174/1568009053332618 · Cited by 103 · see citing works
Increased p53 activity does not accelerate telomere‐driven ageing
García‐Cao, I., García‐Cao, M., Tomás‐Loba, A., Martin‐Caballero, J., Flores, J. M., Klatt, P., Blasco, M. A., & Serrano, M. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400667 · Cited by 102 · cited 1× · see citing works
“Increasing potential p53 activity, by adding an extra copy of p53 or reducing (but not eliminating) expression of Mdm2, resulted in apparently normal mice that were resistant to tumour development (Garcia-Cao et al., 2002, 2006; Mendrysa et al., 2006).”
Background
Regulation of p53 Localization and Activity by Ubc13
Laine, A. M., Topisirović, I., Zhai, D., Reed, J. C., Borden, K. L. B., & Ronai, Z. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01156-06 · Cited by 101 · see citing works
Identification of p53 Sequence Elements That Are Required for MDM2-Mediated Nuclear Export
Gu, J., Nie, L., Wiederschain, D., & Yuan, Z.-M. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8533-8546.2001 · Cited by 100 · see citing works
NMR indicates that the small molecule RITA does not block p53-MDM2 binding in vitro
Krajewski, M., Ozdowy, P., D’Silva, L., Rothweiler, U., & Holak, T. A. (2005) · Nature Medicine · doi:10.1038/nm1105-1135 · Cited by 96 · see citing works
Unleashing the power of p53: lessons from mice and men: Figure 1.Preprint
Poyurovsky, M. V., & Prives, C. L. (2006) · Genes & Development · doi:10.1101/gad.1397506 · Cited by 96 · see citing works
Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function
Andrews, P., He, Y. J., & Xiong, Y. (2006) · Oncogene · doi:10.1038/sj.onc.1209490 · Cited by 95 · see citing works
Overexpression of p 28/ gankyrin in human hepatocellular carcinoma and its clinical significance
Fu, X. (2002) · World Journal of Gastroenterology · doi:10.3748/wjg.v8.i4.638 · Cited by 91 · see citing works
Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)
Megidish, T., Xu, J., & Xu, C. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200001200 · Cited by 89 · see citing works
Human PIRH2 Enhances Androgen Receptor Signaling through Inhibition of Histone Deacetylase 1 and Is Overexpressed in Prostate Cancer
Logan, I. R., Gaughan, L., McCracken, S. R., Sapountzi, V., Leung, H. Y., & Robson, C. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00147-06 · Cited by 88 · see citing works
CARPs Are Ubiquitin Ligases That Promote MDM2-independent p53 and Phospho-p53ser20 Degradation
Yang, W., Rozan, L. M., McDonald, E. R., Navaraj, A., Liu, J. J., Matthew, E. M., Wang, W., Dicker, D. T., & El‐Deiry, W. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610793200 · Cited by 88 · see citing works
The Oncoprotein Gankyrin Negatively Regulates Both p53 and RB by Enhancing Proteasomal Degradation
Higashitsuji, H., Liu, Y., Mayer, R. J., & Fujita, J. (2005) · Cell Cycle · doi:10.4161/cc.4.10.2107 · Cited by 82 · see citing works
WWP1-dependent ubiquitination and degradation of the lung Krüppel-like factor, KLF2
Zhang, X., Srinivasan, S. V., & Lingrel, J. B. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.02.033 · Cited by 78 · see citing works
Ubiquitin and Ubiquitin-Like Modifications of the p53 Family
Watson, I. R., & Irwin, M. S. (2006) · Neoplasia · doi:10.1593/neo.06439 · Cited by 76 · see citing works
p53 Proteasomal Degradation: Poly-Ubiquitination is Not the Whole Story
Asher, G., & Shaul, Y. (2005) · Cell Cycle · doi:10.4161/cc.4.8.1900 · Cited by 73 · see citing works
SUMO-specific protease SUSP4 positively regulates p53 by promoting Mdm2 self-ubiquitination
Lee, M. H., Lee, S. W., Lee, E. J., Choi, S. J., Chung, S. S., Lee, J. I., Cho, J. M., Seol, J. H., Baek, S. H., Kim, K. I., et al. (2006) · Nature Cell Biology · doi:10.1038/ncb1512 · Cited by 70 · see citing works
E6AP Mediates Regulated Proteasomal Degradation of the Nuclear Receptor Coactivator Amplified in Breast Cancer 1 in Immortalized Cells
Mani, A., Oh, A. S., Bowden, E. T., Lahusen, T. J., Lorick, K. L., Weissman, A. M., Schlegel, R., Wellstein, A., & Riegel, A. T. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0557 · Cited by 70 · see citing works
A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis
Nelson, V., Davis, G. E., & Maxwell, S. A. (2001) · APOPTOSIS · doi:10.1023/a:1011392811628 · Cited by 69 · see citing works
Regulation of p53 and MDM2 Activity by MTBP
Brady, M., Vlatković, N., & Boyd, M. T. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.545-553.2005 · Cited by 69 · see citing works
Functional Analysis of p53 Binding under Differential Stresses
Krieg, A. J., Hammond, E. M., & Giaccia, A. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00322-06 · Cited by 66 · see citing works
ATM complexes with HDM2 and promotes its rapid phosphorylation in a p53-independent manner in normal and tumor human cells exposed to ionizing radiation
de Toledo, S. M., Azzam, E. I., Dahlberg, W. K., Gooding, T. B., & Little, J. B. (2000) · Oncogene · doi:10.1038/sj.onc.1204020 · Cited by 64 · see citing works
Human MDM2 Isoforms Translated Differentially on Constitutive versus p53-Regulated Transcripts Have Distinct Functions in the p53/MDM2 and TSG101/MDM2 Feedback Control Loops
Cheng, T.-H., & Cohen, S. N. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00235-06 · Cited by 62 · see citing works
Novel cancer therapy by reactivation of the p53 apoptosis pathway
Bykov, V. J. N., & Wiman, K. G. (2003) · Annals of Medicine · doi:10.1080/07853890310017152 · Cited by 51 · see citing works
Drosophila Topors Is a RING Finger-containing Protein That Functions as a Ubiquitin-protein Isopeptide Ligase for the Hairy Basic Helix-Loop-Helix Repressor Protein
Secombe, J., & Parkhurst, S. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310097200 · Cited by 21 · see citing works
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Engineered Luciferase Reporter from a Deep Sea Shrimp Utilizing a Novel Imidazopyrazinone Substrate
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Restoring synovial homeostasis in rheumatoid arthritis by targeting fibroblast-like synoviocytes
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Are Structural Analogues to Bisphenol A Safe Alternatives?
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p53 modifications: exquisite decorations of the powerful guardian
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The rebel angel: mutant p53 as the driving oncogene in breast cancer
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Cellular Stress Response Pathway System as a Sentinel Ensemble in Toxicological Screening
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5S Ribosomal RNA Is an Essential Component of a Nascent Ribosomal Precursor Complex that Regulates the Hdm2-p53 Checkpoint
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Role of DJ-1 in the mechanism of pathogenesis of Parkinson's disease
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Surf the Post-translational Modification Network of p53 Regulation
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The in vivo gene expression signature of oxidative stress
Han, E., Müller, F. L., Pérez, V., Qi, W., Liang, H., Liang, X., Fu, C., Doyle, E., Hickey, M., Cornell, J. E., et al. (2008) · Physiological Genomics · doi:10.1152/physiolgenomics.00239.2007 · Cited by 236 · see citing works
Butyrate modulates bacterial adherence on LS174T human colorectal cells by stimulating mucin secretion and MAPK signaling pathway
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Deconstructing networks of p53-mediated tumor suppression in vivo
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The Consequences of Chromosome Segregation Errors in Mitosis and Meiosis
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Relevance of the p53–MDM2 axis to aging
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miR-380-5p represses p53 to control cellular survival and is associated with poor outcome in MYCN-amplified neuroblastoma
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20 years studying p53 functions in genetically engineered mice
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HIF-1 antagonizes p53-mediated apoptosis through a secreted neuronal tyrosinase
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Characterization of genome-wide p53-binding sites upon stress response
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Cancer and ageing: convergent and divergent mechanisms
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p53 Regulation of Metabolic PathwaysPreprint
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SnapShot: p53 Posttranslational Modifications
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Aneuploidy and chromosomal instability: a vicious cycle driving cellular evolution and cancer genome chaos
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Emerging Disinfection Byproducts, Halobenzoquinones: Effects of Isomeric Structure and Halogen Substitution on Cytotoxicity, Formation of Reactive Oxygen Species, and Genotoxicity
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The Central Nervous System-Restricted Transcription Factor Olig2 Opposes p53 Responses to Genotoxic Damage in Neural Progenitors and Malignant Glioma
Mehta, S. V., Huillard, E., Kesari, S., Maire, C. L., Golebiowski, D., Harrington, E. P., Alberta, J. A., Kane, M., Theisen, M., Ligon, K. L., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.035 · Cited by 158 · see citing works
Caspase-2-Mediated Cleavage of Mdm2 Creates a p53-Induced Positive Feedback Loop
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Biotin conjugated organic molecules and proteins for cancer therapy: A review
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Homeostatic functions of the p53 tumor suppressor: Regulation of energy metabolism and antioxidant defense
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Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer
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Merkel cell carcinoma
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Another fork in the road—life or death decisions by the tumour suppressor p53
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Chloroquine activates the p53 pathway and induces apoptosis in human glioma cells
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Regulation of Cellular Metabolism and Hypoxia by p53Preprint
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Genetics and Epigenetics of Human Retinoblastoma
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Radioprotective Agents: Strategies and Translational Advances
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The cell death machinery governed by the p53 tumor suppressor in response to DNA damage
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Cyclin-Dependent Kinase Inhibitors as Anticancer Drugs
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The disulfide compound α-lipoic acid and its derivatives: A novel class of anticancer agents targeting mitochondria
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Induction of SOX4 by DNA damage is critical for p53 stabilization and function
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Acquisition of p53 mutations in response to the non-genotoxic p53 activator Nutlin-3
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Cop1 constitutively regulates c-Jun protein stability and functions as a tumor suppressor in mice
Migliorini, D., Bogaerts, S., Defever, D., Vyas, R., Denecker, G., Radaelli, E., Zwolińska, A., Depaepe, V., Hochepied, T., Skarnes, W. C., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45784 · Cited by 128 · see citing works
Cell Cycle Regulation by the Nutrient-Sensing Mammalian Target of Rapamycin (mTOR) Pathway
Cuyàs, E., Corominas-Faja, B., Joven, J., & Menéndez, J. A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0888-2_7 · Cited by 125 · see citing works
Mdm2 Induces Mono-Ubiquitination of FOXO4
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P53 in kidney injury and repair: Mechanism and therapeutic potentials
Tang, C., Ma, Z., Zhu, J., Liu, Z., Liu, Y., Liu, Y., Cai, J., & Dong, Z. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.10.013 · Cited by 121 · see citing works
Regulation of p53 stability and function by the deubiquitinating enzyme USP42
Hock, A. K., Vigneron, A. M., Carter, S., Ludwig, R. L., & Vousden, K. H. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.419 · Cited by 117 · see citing works
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Spotlight on the role of COP1 in tumorigenesis
Marine, J. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3271 · Cited by 118 · see citing works
Cytochrome P450 2E1 (CYP2E1) regulates the response to oxidative stress and migration of breast cancer cells
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p53 and ATF4 mediate distinct and additive pathways to skeletal muscle atrophy during limb immobilization
Fox, D. K., Ebert, S. M., Bongers, K. S., Dyle, M. C., Bullard, S. A., Dierdorff, J. M., Kunkel, S. D., & Adams, C. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00010.2014 · Cited by 119 · see citing works
P53 Dysfunction in Neurodegenerative Diseases - The Cause or Effect of Pathological Changes?
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Liquiritin induces apoptosis and autophagy in cisplatin (DDP)-resistant gastric cancer cells in vitro and xenograft nude mice in vivo
Feng, W., Jiang, X. M., Gao, H., & Gao, S. (2017) · International Journal of Oncology · doi:10.3892/ijo.2017.4134 · Cited by 115 · see citing works
SOX4 overexpression regulates the p53-mediated apoptosis in hepatocellular carcinoma: clinical implication and functional analysis in vitro
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Depletion of the novel p53-target gene carnitine palmitoyltransferase 1C delays tumor growth in the neurofibromatosis type I tumor model
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Nucleolar stress: From development to cancer
Lafita‐Navarro, M. C., & Conacci‐Sorrell, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.04.001 · Cited by 109 · see citing works
Upregulation and activation of p53 by erastin‑induced reactive oxygen species contribute to cytotoxic and cytostatic effects in A549 lung cancer cells
Huang, C., Yang, M., Deng, J., Li, P., Su, W., & Jiang, R. (2018) · Oncology Reports · doi:10.3892/or.2018.6585 · Cited by 107 · see citing works
SUMOylation of hnRNP‐K is required for p53‐mediated cell‐cycle arrest in response to DNA damage
Lee, S. W., Lee, M. H., Park, J. H., Kang, S. H., Yoo, H. M., Ka, S. H., Oh, Y. M., Jeon, Y. J., & Chung, C. H. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.293 · Cited by 103 · see citing works
Molecular pathogenesis of Merkel cell carcinoma
Houben, R., Schrama, D., & Becker, J. C. (2009) · Experimental Dermatology · doi:10.1111/j.1600-0625.2009.00853.x · Cited by 101 · see citing works
Of the many cellular responses activated by TP53, which ones are critical for tumour suppression?
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Molecular Mechanisms of p53 Deregulation in Cancer: An Overview in Multiple Myeloma
Herrero, A. B., Rojas, E. A., Misiewicz-Krzemińska, I., Krzemiński, P., & Gutierrez, N. C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122003 · Cited by 99 · see citing works
Resveratrol induces cell cycle arrest via a p53-independent pathway in A549 cells
Yuan, L., Zhang, Y., XIA, J., Liu, B., ZHANG, Q., LIU, J., Luo, L., Zhou, P., Song, Z., & Zhu, R. (2014) · Molecular Medicine Reports · doi:10.3892/mmr.2014.3100 · Cited by 98 · see citing works
Mouse Models of p53 FunctionsPreprint
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The Regulation of the p53-mediated Stress Response by MDM2 and MDM4Preprint
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Macrolides induce severe cardiotoxicity and developmental toxicity in zebrafish embryos
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STAT1 deficiency in the heart protects against myocardial infarction by enhancing autophagy
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Resveratrol overcomes gefitinib resistance by increasing the intracellular gefitinib concentration and triggering apoptosis, autophagy and senescence in PC9/G NSCLC cells
Zhu, Y., He, W., Gao, X., Li, B., Mei, C., Xu, R., & Chen, H. (2015) · Scientific Reports · doi:10.1038/srep17730 · Cited by 90 · see citing works
Role of miRNAs in the pathogenesis and susceptibility of diabetes mellitus
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Hyperoxia Impairs Alveolar Formation and Induces Senescence Through Decreased Histone Deacetylase Activity and Up-Regulation of p21 in Neonatal Mouse Lung
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Post-transcriptional Modulation of Iron Homeostasis during p53-dependent Growth Arrest
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Crystal structure of a p53 core tetramer bound to DNA
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p53-Independent Apoptosis Limits DNA Damage-Induced Aneuploidy
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Molecular mechanisms behind ROS regulation in cancer: A balancing act between augmented tumorigenesis and cell apoptosis
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AHNAK controls 53BP1-mediated p53 response by restraining 53BP1 oligomerization and phase separation
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Exaptive Evolution of Target of Rapamycin Signaling in Multicellular Eukaryotes
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Evolutionary landscape of clonal hematopoiesis in 3,359 individuals from the general population
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Dysfunction of the MDM2/p53 axis is linked to premature aging
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Elevated Levels of Oncogenic Protein Kinase Pim-1 Induce the p53 Pathway in Cultured Cells and Correlate with Increased Mdm2 in Mantle Cell Lymphoma
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Self-citation
Activation and activities of the p53 tumour suppressor protein
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Self-citation
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Authors: Horn, H. F., & Vousden, K. H.
Affiliations: Cancer Research UK Scotland Institute (GB)
Corresponding author: Vousden, K H
ORCID: Horn, H F
Vousden, K H
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2007-02-26
Volume: 26
Issue: 9
Pages: 1306-1316
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1210263
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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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Coping with stress: multiple ways to activate p53

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