MDM2 interacts with MDMX through their RING finger domains
Abstract
The N‐terminus of MDM2 proto‐oncoprotein interacts with p53 and down modulates p53 activity by inhibiting transcriptional activity and promoting p53 degradation. MDMX is structurally related to MDM2 and also binds to p53. However, the function of MDMX has not been clarified yet. We found that MDM2 hetero‐oligomerized with MDMX through their C‐terminal RING finger domains. Yeast two‐hybrid analysis revealed that the hetero‐oligomerization between MDMX and MDM2 was more stable than the homo‐oligomerization of each protein. MDM2 has been shown to be degraded by the ubiquitin‐proteasome pathway, while MDMX was a stable protein. Interaction of MDMX with MDM2 through the C‐terminal RING finger domains resulted in inhibiting degradation of MDM2. These data indicate that MDMX functions as a regulator of MDM2.
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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 [26]
The Mdmx mutant lacking the RING domain (MxΔRING) is unable to heterodimerize with Mdm2.
“we generated a deletion mutant of Mdmx (1–345 amino acids) that lacked its RING domain (MxΔRING), and thus, was unable to heterodimerize with Mdm2.26,27”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [26]
The RING domain of Mdmx is required for binding to Mdm2 through its RING domain.
“The RING domain of Mdmx is required to bind to Mdm2 through its RING domain.26,27”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [26]
Mdm2 can homo-oligomerize or hetero-oligomerize with Mdmx via RING/RING interaction, whereas Mdmx alone is monomeric.
“Although Mdm2 can homo-oligomerizea, or hetero-oligomerize with Mdmx via RING/RING interaction, it appears that Mdmx alone is monomeric [17].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [17]
MDMX and MDM2 form heterodimers through their C-terminal RING domains, and the MDM2 RING domain alone is sufficient to degrade MDMX.
“MDMX and MDM2 form heterodimers through the C-terminal RING domains and the MDM2 RING domain alone is sufficient to degrade MDMX (Sharp et al, 1999;Tanimura et al, 1999;Pan and Chen, 2003).”
From ATM and Chk2-dependent phosphorylation of MDMX contribute to p53 activation after DNA damage (2005) · cites this paper as Tanimura et al, 1999
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- Authors
- Tanimura, S., Ohtsuka, S., Mitsui, K., Shirouzu, K., Yoshimura, A., & Ohtsubo, M.
- Affiliations
- Kurume University (JP)
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1999-03-19
- Volume
- 447
- Issue
- 1
- Pages
- 5-9
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2004311983
- Cited by
- 324
- References
- 27
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 6 · 2023: 6 · 2022: 6 · 2021: 8 · 2020: 11 · 2019: 7 · 2018: 9 · 2017: 16 · 2016: 18 · 2015: 9 · 2014: 25 · 2013: 8 · 2012: 19
- FWCI
- 5.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- 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
- MDM2, MDMX, RING domain, protein-protein interaction, hetero-oligomerization, p53, ubiquitin-proteasome system, protein degradation, tumor suppressor proteins
- MeSH terms
- Binding Sites, Cloning, Molecular, Nuclear Proteins, Protein Binding, Protein Conformation, Proto-Oncogene Proteins, Recombinant Proteins, Saccharomyces cerevisiae, Tumor Suppressor Protein p53, Zinc Fingers, Proto-Oncogene Proteins c-mdm2
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