Regulation of p53: a collaboration between Mdm2 and MdmX
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Dongsheng Pei 1,2 , Yanping Zhang 1,2 and Junnian Zheng 1 1 Laboratory of Biological Cancer Therapy, Xuzhou Medical College, Xuzhou, China 2 Department of Radiation Oncology and Lineberger Comprehensive Cancer Center, School of Medicine, the University of North Carolina at Chapel Hill, Chapel Hill, NC, USA Received: February 17, 2012; Accepted: March 2, 2012; Published: March 10, 2012; Keywords: Mdm2, MdmX, p53, cancer Correspondence: Yanping Zhang, // Junnian Zheng, // // Abstract p53 plays an important role in the regulation of the cell cycle, DNA repair, and apoptosis and is an attractive cancer therapeutic target. Mdm2 and Mdmx are recognized as the main p53 negative regulators. Although it remains unclear why Mdm2 and Mdmx are both required for p53 degradation, a model has been proposed whereby these two proteins function independent of one another; Mdm2 acts as an E3 ubiquitin ligase that catalyzes the ubiquitination of p53 for degradation, whereas Mdmx inhibits p53 by binding to and masking the transcriptional activation domain of p53, without causing its degradation. However, Mdm2 and Mdmx have been shown to function collaboratively. In fact, recent studies have pointed to a more important role for an Mdm2/Mdmx co-regulatory mechanism of p53 regulation than previously thought. In this review, we summarize current progress in the field about the functional and physical interaction between Mdm2 and Mdmx, their individual and collaborative roles in controlling p53, and inhibitors that target Mdm2 and Mdmx as a novel class of anticancer therapeutics.
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Through their RING domains, Mdmx binds Mdm2 and enhances Mdm2's ability to regulate p53.
“Additionally, it has been shown that through their RING domains, Mdmx binds Mdm2 and enhances the ability of Mdm2 to regulate p53.23,24,26–28”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [28]
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- Authors
- Pei, D., Zhang, Y., & Zheng, J.
- Affiliations
- Laboratory of Biological Cancer Therapy, Xuzhou Medical College, Xuzhou, China
- University of North Carolina at Chapel Hill (US)
- Xuzhou Medical College (CN)
- Venue
- Oncotarget
- Publisher
- Impact Journals, LLC
- Published
- 2012-03-10
- Volume
- 3
- Issue
- 3
- Pages
- 228-235
- ISSN
- 1949-2553 (ISSN-L)
- PMC
- PMC3359881
- OpenAlex
- W1868102126
- Cited by
- 140
- References
- 75
- Citations by year
- 2026: 6 · 2025: 7 · 2023: 4 · 2022: 6 · 2021: 7 · 2020: 6 · 2019: 10 · 2018: 10 · 2017: 9 · 2016: 18 · 2015: 12 · 2014: 23 · 2013: 17 · 2012: 5
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Oncotarget (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01CA167637, R01CA100302, R01CA127770)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- p53 regulation, MDM2, MDMX, p53 degradation, E3 ubiquitin ligase, ubiquitination, MDM2 inhibitors, anticancer agents, tumor suppressor
- MeSH terms
- Animals, Humans, Models, Biological, Nuclear Proteins, Protein Binding, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Gene Expression Regulation, Neoplastic, Tumor Suppressor Protein p53, Cell Cycle Proteins, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Protein Stability
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