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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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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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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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