Acetylation-dependent regulation of MDM2 E3 ligase activity dictates its oncogenic function.
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, thereby promoting self-ubiquitination and less ubiquitination and subsequent degradation of p53, thus increasing p53-dependent apoptosis. Therefore, this study indicates that dynamic acetylation is a molecular switch in the regulation of MDM2 substrate specificity, revealing further insight into the posttranslational regulation of the MDM2/p53 cell survival axis.
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Deacetylation of Mdm2 by Sirt1 contributes to the Mdm2/p53 switch by disrupting Mdm2-USP7 association, leading to Mdm2 auto-ubiquitination.
“Deacetylation of Mdm2 by Sirt1 also contributes to the Mdm2/p53 switch, by disrupting the association between Mdm2 and USP7, leading to Mdm2 auto-ubiquitination (Nihira et al., 2017).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Nihira et al., 2017
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References 47 · Cited by 82
Research works printed but not linked: 1
- [6]Bartel F Meye A Würl P Kappler M Bache M Lautenschläger C Grünbaum U Schmidt H Taubert H Amplification of the MDM2 gene, but not expression of splice variants of MDM2 MRNA, is associated with prognosis in soft tissue sarcoma Int J Cancer 95 168 175 2001 11307150
- Authors
- Nihira, N. T., Ogura, K., Shimizu, K., North, B. J., Zhang, J., Gao, D., Inuzuka, H., & Wei, W.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Corresponding author
- Inuzuka, Hiroyuki
- Wei, Wenyi
- ORCID
- Venue
- Science Signaling
- Published
- 2017-02-14
- Volume
- 10
- Issue
- 466
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- PMC
- PMC5468793
- OpenAlex
- W2588201113
- Cited by
- 82
- References
- 47
- Citations by year
- 2026: 5 · 2025: 13 · 2024: 6 · 2023: 9 · 2022: 11 · 2021: 7 · 2020: 8 · 2019: 10 · 2018: 8 · 2017: 5
- FWCI
- 3.74
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science Signaling (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (award290163)
- National Cancer Institute (award290164)
- National Institute of General Medical Sciences (award290165)
- 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, acetylation, E3 ubiquitin ligase, p53, post-translational modification, substrate specificity, p53 degradation, apoptosis, oncogenic function, cell survival
- MeSH terms
- A549 Cells, Ubiquitin-Specific Peptidase 7, p300-CBP-Associated Factor, Acetylation, Cell Transformation, Neoplastic, Humans, Lysine, Oncogenes, Protein Binding, Immunoblotting, Tumor Suppressor Protein p53, RNA Interference, HCT116 Cells, Cell Line, Tumor, p300-CBP Transcription Factors, Proto-Oncogene Proteins c-mdm2, Ubiquitination, Sirtuin 1, HEK293 Cells, MCF-7 Cells
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