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Multisite aggregation of p53 and implications for drug rescue
Abstract
Significance: Destabilized mutants of the tumor suppressor p53 are inactivated by self-aggregation in a substantial number of tumors and may also coaggregate with and inactivate WT p53 and family members. We found in vitro that self-aggregation proceeded via a network of multiple aggregation-prone sites in p53, and inhibition of an individual site did not inhibit aggregation. Nevertheless, peptides designed to be complementary to various aggregation sequences and inhibit their polymerization can specifically kill cancer cells and be potential anticancer drugs. We found that those peptides can also function by p53-independent routes in cancer cell cultures, implying further therapeutic targets.
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“In p53-silenced cells, the response of ReACp53 was not abolished, and addition of this peptide to p53-silenced two-dimensional cultured cancer cells resulted in rapid apoptosis.495”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [495]
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“Mutant p53 aggregates not only induced wild-type p53 aggregates but also coaggregated with p63 and p73495,500”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [495]
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Cited by
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
(2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.002 · Cited by 78
p53: from understanding its structure to advances in therapeutic targeting
Wang, W., Liu, X., Liu, H., Abolhassani, H., Yan, H., Zhang, H., & Wang, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02549-5 · Cited by 30
Yin, Z.-X., Hang, W., Liu, G., Wang, Y.-S., Shen, X.-F., Sun, Q.-H., Li, D.-D., Jian, Y.-P., Zhang, Y.-H., Quan, C.-S., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.21277 · Cited by 19
Metadata
- Authors
- Wang, G., & Fersht, A. R.
- Affiliations
- MRC Laboratory of Molecular Biology, PNAC Division, Cambridge CB2 0QH, United Kingdom
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2017-03-14
- Volume
- 114
- Issue
- 13
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 54
- References
- 8
- Language
- en
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