The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
p53 regulation by ubiquitin
Open accessAbstract
The ubiquitination pathway is a highly dynamic and coordinated process that regulates degradation as well as numerous processes of proteins within a cell. The p53 tumor suppressor and several factors in the pathway are regulated by ubiquitin as well as ubiquitin-like proteins. These modifications are critical for the function of p53 and control both the degradation of the protein as well as localization and activity. Importantly, more recent studies have identified deubiquitination enzymes that can specifically remove ubiquitin moieties from p53 or other factors in the pathway, and the reversible nature of this process adds yet another layer of regulatory control of p53. This review highlights the recent advances in our knowledge of ubiquitin and the p53 pathway.
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“Mdm2 typically functions as an E3 ubiquitin ligase and conjugates ubiquitin to several proteins including, the tumor suppressor p53. This ultimately signals for destruction by the 26S proteasome to keep cellular p53 levels low [1,2].”
From Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis (2012) · cites this paper as [1]
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1 retracted
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
RetractedHershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
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
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 1×
“Shortly thereafter, Mdm2 was identified as a cellular factor that ubiquitinates and degrades p53 in the absence of exogenous factors [6–8].”
BackgroundMechanisms Underlying Ubiquitination
Pickart, C. M. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.503 · Cited by 3,184
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
Xue, W., Zender, L., Miething, C., Dickins, R. A., Hernando, E., Krizhanovsky, V., Cordon-Cardo, C., & Lowe, S. W. (2007) · Nature · doi:10.1038/nature05529 · Cited by 2,473
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108 · cited 1×
“The formation of a pore in the membrane allows for the release of cytochrome c and other apoptotic factors into the cytoplasm [45–47].”
BackgroundOncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951
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Gutschner, T., & Diederichs, S. (2012) · RNA Biology · doi:10.4161/rna.20481 · Cited by 1,844
MEG3 noncoding RNA: a tumor suppressor
Zhou, Y., Zhang, X., & Klibanski, A. (2012) · Journal of Molecular Endocrinology · doi:10.1530/jme-12-0008 · Cited by 724
Regulation of DNA Damage Responses by Ubiquitin and SUMO
Jackson, S. P., & Durocher, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.017 · Cited by 601
Roey, K. V., Uyar, B., Weatheritt, R. J., Dinkel, H., Seiler, M., Budd, A., Gibson, T. J., & Davey, N. E. (2014) · Chemical Reviews · doi:10.1021/cr400585q · Cited by 513
Oncogenic lncRNA downregulates cancer cell antigen presentation and intrinsic tumor suppression
Hu, Q., Ye, Y., Chan, L.-C., Li, Y., Liang, K., Lin, A., Egranov, S. D., Zhang, Y., Xia, W., Gong, J., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0400-7 · Cited by 353
Metadata
- Authors
- Brooks, C. L., & Gu, W.
- Affiliations
- Stemline Therapeutics (United States) (US)
- Columbia University (US)
- Corresponding author
- Brooks, Christopher L.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2011-05-27
- Volume
- 585
- Issue
- 18
- Pages
- 2803-2809
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- PMC
- PMC3172401
- OpenAlex
- W2079076511
- Cited by
- 186
- References
- 96
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 9 · 2023: 14 · 2022: 8 · 2021: 15 · 2020: 13 · 2019: 12 · 2018: 9 · 2017: 18 · 2016: 14 · 2015: 13 · 2014: 16 · 2013: 18 · 2012: 17
- FWCI
- 1.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- FEBS Letters (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, R01CA118561, P01CA080058, R01CA129627)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- p53, ubiquitination, ubiquitin, deubiquitination, protein degradation, tumor suppressor regulation, ubiquitin-like proteins, protein localization, protein function regulation
- MeSH terms
- Animals, Humans, Models, Biological, Transcriptional Activation, Tumor Suppressor Protein p53, Active Transport, Cell Nucleus, Ubiquitin, Proteasome Endopeptidase Complex, Proto-Oncogene Proteins c-mdm2, Ubiquitination
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