Proteasome machinery is instrumental in a common gain-of-function program of the p53 missense mutants in cancer
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In cancer, the tumour suppressor gene TP53 undergoes frequent missense mutations that endow mutant p53 proteins with oncogenic properties. Until now, a universal mutant p53 gain-of-function program has not been defined. By means of multi-omics: proteome, DNA interactome (chromatin immunoprecipitation followed by sequencing) and transcriptome (RNA sequencing/microarray) analyses, we identified the proteasome machinery as a common target of p53 missense mutants. The mutant p53-proteasome axis globally affects protein homeostasis, inhibiting multiple tumour-suppressive pathways, including the anti-oncogenic KSRP-microRNA pathway. In cancer cells, p53 missense mutants cooperate with Nrf2 (NFE2L2) to activate proteasome gene transcription, resulting in resistance to the proteasome inhibitor carfilzomib. Combining the mutant p53-inactivating agent APR-246 (PRIMA-1MET) with the proteasome inhibitor carfilzomib is effective in overcoming chemoresistance in triple-negative breast cancer cells, creating a therapeutic opportunity for treatment of solid tumours and metastasis with mutant p53.
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Activation of p53 in some cases may have the opposite effect.
“indicating that activation of p53 in some cases may have the opposite effect, which was consistent with results from other studies [94–96].”
From Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials (2022) · cites this paper as [96]
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- Authors
- Walerych, D., Lisek, K., Sommaggio, R., Piazza, S., Ciani, Y., Dalla, E., Rajkowska, K., Gaweda-Walerych, K., Ingallina, E., Tonelli, C., Morelli, M. J., Amato, A., Eterno, V., Zambelli, A., Rosato, A., Amati, B., Wiśniewski, J. R., & Del Sal, G.
- Affiliations
- AREA Science Park (IT)
- University of Trieste (IT)
- University of Padua (IT)
- European Institute of Oncology (IT)
- Italian Institute of Technology (IT)
- Istituti Clinici Scientifici Maugeri (IT)
- Max Planck Institute of Biochemistry (DE)
- ORCID
- Venue
- Nature Cell Biology
- Published
- 2016-06-27
- Volume
- 18
- Issue
- 8
- Pages
- 897-909
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2460207510
- Cited by
- 239
- References
- 70
- Citations by year
- 2026: 12 · 2025: 11 · 2024: 16 · 2023: 21 · 2022: 26 · 2021: 25 · 2020: 36 · 2019: 25 · 2018: 28 · 2017: 29 · 2016: 8 · 2015: 1
- FWCI
- 16.18
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Institutional Research Information System (University of Udine) (submittedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion, other-oa)
- BOA (University of Milano-Bicocca) (submittedVersion)
- Max Planck Digital Library (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Padua Research Archive (University of Padova) (submittedVersion, other-oa)
- 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
- TP53 missense mutations, proteasome, Nrf2, APR-246, PRIMA-1MET, proteostasis, triple-negative breast cancer, chemoresistance, combination therapy, tumor suppressor inactivation
- MeSH terms
- Animals, Antineoplastic Agents, Humans, Neoplasm Metastasis, Oligopeptides, Quinuclidines, Tumor Suppressor Protein p53, Mutation, Missense, Proteome, MicroRNAs, Proteasome Endopeptidase Complex, Mutant Proteins, NF-E2-Related Factor 2, Mice, Triple Negative Breast Neoplasms
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