Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway
Open accessAbstract
The tumor suppressor p53 and its homologues, p63 and p73, play a pivotal role in the regulation of the DNA damage response, cellular homeostasis, development, aging, and metabolism. A number of mouse studies have shown that a genetic defect in the p53 family could lead to spontaneous tumor development, embryonic lethality, or severe tissue abnormality, indicating that the activity of the p53 family must be tightly regulated to maintain normal cellular functions. While the p53 family members are regulated at the level of gene expression as well as post-translational modification, they are also controlled at the level of protein stability through the ubiquitin proteasomal pathway. Over the last 20 years, many ubiquitin E3 ligases have been discovered that directly promote protein degradation of p53, p63, and p73 in vitro and in vivo. Here, we provide an overview of such E3 ligases and discuss their roles and functions.
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MDM2 can cooperate with MDMX to kinetically enhance p53 polyubiquitination, resulting in p53 stability and tumor occurrence.
“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 [12]
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- Authors
- Bang, S., Kaur, S., & Kurokawa, M.
- Affiliations
- Kent State University (US)
- Corresponding author
- Kurokawa, Manabu
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2019-12-30
- Volume
- 21
- Issue
- 1
- Pages
- 261
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6981958
- OpenAlex
- W2997391651
- Cited by
- 69
- References
- 262
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 10 · 2023: 10 · 2022: 7 · 2021: 12 · 2020: 14
- FWCI
- 0.79
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (R00 CA140948, R03 CA230828)
- 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 family, p63, p73, E3 ubiquitin ligase, protein degradation, protein stability, tumor suppressor regulation, DNA damage response, post-translational modification
- MeSH terms
- Tumor Protein p73, Animals, Humans, Neoplasms, Protein Processing, Post-Translational, Trans-Activators, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Mice, Proteolysis
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