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The role of ubiquitin modification in the regulation of p53
Open accessAbstract
The p53 tumor suppressor protein is involved in regulating a wide variety of stress responses, from senescence and apoptosis to more recently discovered roles in allowing adaptation to metabolic and oxidative stress. After 34years of research, significant progress has been made in unraveling the complexity of the p53 network, and it is clear that the regulation of p53 protein stability is critical in the control of p53 activity. This article focuses on our current understanding of how the level and activity of p53 is controlled by this seemingly simple mechanism. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.
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“MDM2 can cooperate with MDMX (mouse double minute X) to kinetically enhance p53 polyubiquitination, resulting in p53 stability and the occurrence of tumors [11–13].”
From Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials (2022) · cites this paper as [11]
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Kurki, S., Latonen, L., & Laiho, M. (2003) · Journal of Cell Science · doi:10.1242/jcs.00714 · Cited by 91
Migliorini, D., Danovi, D., Colombo, E., Carbone, R., Pelicci, P. G., & Marine, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108795200 · Cited by 88
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
Regulation of p53 family members by the ubiquitin-like SUMO system
Stehmeier, P., & Muller, S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.002 · Cited by 83
Validation of MdmX as a therapeutic target for reactivating p53 in tumors
Garcia, D., Warr, M. R., Martins, C. P., Brown Swigart, L., Passegué, E., & Evan, G. I. (2011) · Genes & Development · doi:10.1101/gad.16722111 · Cited by 83
Regulation of MDMX Expression by Mitogenic Signaling
Gilkes, D. M., Pan, Y., Coppola, D., Yeatman, T., Reuther, G. W., & Chen, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01633-07 · Cited by 82
Scission of the p53-MDM2 Loop by Ribosomal Proteins
Zhou, X. Y., Liao, J.-M., Liao, W.-J., & Lu, H. (2012) · Genes & Cancer · doi:10.1177/1947601912455200 · Cited by 82
Nie, J., Xie, P., Liu, L., Xing, G., Chang, Z., Yin, Y., Tian, C., He, F., & Zhang, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.126920 · Cited by 79
Phosphorylation of MDMX Mediated by Akt Leads to Stabilization and Induces 14-3-3 Binding
Lopez-Pajares, V., Kim, M. M., & Yuan, Z.-M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710030200 · Cited by 79
JFK, a Kelch domain-containing F-box protein, links the SCF complex to p53 regulation
Sun, L., Shi, L., Li, W., Yu, W., Liang, J., Zhang, H., Yang, X., Wang, Y., Li, R., Yao, X., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901864106 · Cited by 79
Flagged first, then by citations
6 of the 275 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Autophagy in malignant transformation and cancer progression
Galluzzi, L., Pietrocola, F., Bravo‐San Pedro, J. M., Amaravadi, R. K., Baehrecke, E. H., Cecconi, F., Codogno, P., Debnath, J., Gewirtz, D. A., Karantza, V., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201490784 · Cited by 1,182
P53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080
Self-citationControl of protein stability by post-translational modifications
Lee, J. M., Hammarén, H. M., Savitski, M. M., & Baek, S. H. (2023) · Nature Communications · doi:10.1038/s41467-023-35795-8 · Cited by 896
Soussi, T., & Wiman, K. G. (2015) · Cell Death & Differentiation · doi:10.1038/cdd.2015.53 · Cited by 305
Therapeutic strategies to overcome taxane resistance in cancer
Das, T., Anand, U., Pandey, S. K., Ashby, C. R., Assaraf, Y. G., Chen, Z., & Dey, A. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100754 · Cited by 262
Metadata
- Authors
- Hock, A. K., & Vousden, K. H.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Corresponding author
- Vousden, Karen H.
- ORCID
- Vousden, Karen H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 1843
- Issue
- 1
- Pages
- 137-149
- ISSN
- 0167-4889 (ISSN-L)
- OpenAlex
- W2062976534
- Cited by
- 168
- References
- 275
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 12 · 2021: 27 · 2020: 9 · 2019: 9 · 2018: 15 · 2017: 17 · 2016: 18 · 2015: 19 · 2014: 15
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- CR-UK
- 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 › Heat shock proteins research
- Keywords
- p53, ubiquitin modification, protein stability, ubiquitin-proteasome system, tumor suppressor regulation, apoptosis, senescence, oxidative stress, metabolic stress, stress response
- MeSH terms
- Animals, Humans, Protein Processing, Post-Translational, Transcriptional Activation, Tumor Suppressor Protein p53, Ubiquitin, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Protein Stability
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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