Cited by 187Ubiquitin and proteasome pathwaysCancer-related Molecular PathwaysTGF-β signaling in diseases

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p53 regulation by ubiquitin

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Brooks, Christopher L., Gu, Wei·2011·FEBS Letters

DOI 10.1016/j.febslet.2011.05.022PMC PMC3172401

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Abstract

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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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
Retracted
THE UBIQUITIN SYSTEM
Hershko, 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].”
Background
Mechanisms 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].”
Background
Oncoprotein 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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Authors: Brooks, C. L., & Gu, W.
Affiliations: Stemline Therapeutics (United States) (US)
Columbia University (US)
Corresponding author: Brooks, Christopher L.
ORCID: Brooks, Christopher L.
Gu, Wei
Venue: FEBS Letters
Publisher: Wiley
Published: 2011-05-27
Volume: 585
Issue: 18
Pages: 2803-2809
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/j.febslet.2011.05.022
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
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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