The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Acetylation Is Crucial for p53-Mediated Ferroptosis and Tumor Suppression
Open accessAbstract
Although previous studies indicate that loss of p53-mediated cell cycle arrest, apoptosis, and senescence does not completely abrogate its tumor suppression function, it is unclear how the remaining activities of p53 are regulated. Here, we have identified an acetylation site at lysine K98 in mouse p53 (or K101 for human p53). Whereas the loss of K98 acetylation (p53 K98R ) alone has very modest effects on p53-mediated transactivation, simultaneous mutations at all four acetylation sites (p53 4KR : K98R+ 3KR[K117R+K161R+K162R]) completely abolish its ability to regulate metabolic targets, such as TIGAR and SLC7A11. Notably, in contrast to p53 3KR , p53 4KR is severely defective in suppressing tumor growth in mouse xenograft models. Moreover, p53 4KR is still capable of inducing the p53-Mdm2 feedback loop, but p53-dependent ferroptotic responses are markedly abrogated. Together, these data indicate the critical role of p53 acetylation in ferroptotic responses and its remaining tumor suppression activity.
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“p53 was reported to inhibit cystine uptake and promote ferroptosis by transcriptional repression the expression of SLC7A11”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [126]
In the citing paper
“Another mutant of p53(4KR) lost the ability to regulate SLC7A11 expression.126”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [126]
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Cites
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398
Self-citationBlinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Glutaminolysis and transferrin regulate ferroptosis
Gao, M., Monian, P., Quadri, N., Ramasamy, R., & Jiang, X. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.06.011 · Cited by 2,069
The first 30 years of p53: growing ever more complex.
Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610 · cited 1×
“…include p53 protein stability, co-activator and inhibitor recruitment, and a diverse array of posttranslational modifications, including acetylation, ubiquitination, phosphorylation, methylation, sumoylation, and neddylation (Eischen and Lozano, 2014; Gannon and Jones, 2012; Kruse and Gu, 2009).”
BackgroundSelf-citationTumor Suppression in the Absence of p53-Mediated Cell-Cycle Arrest, Apoptosis, and Senescence
Li, T., Kon, N., Jiang, L., Tan, M., Ludwig, T., Zhao, Y., Baer, R., & Gu, W. (2012) · Cell · doi:10.1016/j.cell.2012.04.026 · Cited by 912
Self-citationGlutaminase 2, a novel p53 target gene regulating energy metabolism and antioxidant function
Hu, W., Zhang, C., Wu, R., Sun, Y., Levine, A., & Feng, Z. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001006107 · Cited by 862
Acetylation Is Indispensable for p53 Activation
Tang, Y., Zhao, W., Chen, Y., Zhao, Y., & Gu, W. (2008) · Cell · doi:10.1016/j.cell.2008.03.025 · Cited by 838
Self-citationAcetylation of the p53 DNA-binding domain regulates apoptosis induction.
Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752
Cited by
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252
Role of Mitochondria in Ferroptosis
Gao, M., Yi, J., Zhu, J., Minikes, A. M., Monian, P., Thompson, C. B., & Jiang, X. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.10.042 · Cited by 2,120
Ferroptosis at the crossroads of cancer-acquired drug resistance and immune evasion
Friedmann Angeli, J. P., Krysko, D. V., & Conrad, M. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0149-1 · Cited by 1,259
The development of the concept of ferroptosis
Hirschhorn, T., & Stockwell, B. R. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.043 · Cited by 1,052
Metadata
- Authors
- Wang, S.-J., Li, D., Ou, Y., Jiang, L., Chen, Y., Zhao, Y., & Gu, W.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2016-10
- Volume
- 17
- Issue
- 2
- Pages
- 366-373
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2529409645
- Cited by
- 462
- References
- 30
- FWCI
- 10.82
- Type
- journal article
- Language
- en
- Open access
- gold
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- Wang, S.-J., Li, D., Ou, Y., Jiang, L., Chen, Y., Zhao, Y., & Gu, W. (2016). Acetylation Is Crucial for p53-Mediated Ferroptosis and Tumor Suppression. Cell Reports. https://doi.org/10.1016/j.celrep.2016.09.022
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
