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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Tip60-Dependent Acetylation of p53 Modulates the Decision between Cell-Cycle Arrest and Apoptosis
Tang, Y., Luo, J., Zhang, W., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.021 · Cited by 727
Self-citationSuzuki, S., Tanaka, T., Poyurovsky, M. V., Nagano, H., Mayama, T., Ohkubo, S., Lokshin, M., Hosokawa, H., Nakayama, T., Suzuki, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002459107 · Cited by 705
Distinct p53 Transcriptional Programs Dictate Acute DNA-Damage Responses and Tumor Suppression
Brady, C. A., Jiang, D., Mello, S. S., Johnson, T. M., Jarvis, L. A., Kozak, M. M., Broz, D. K., Basak, S., Park, E. J., McLaughlin, M. E., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.035 · Cited by 533
Choudhury, A. R., Ju, Z., Djojosubroto, M. W., Schienke, A., Lechel, A., Schaetzlein, S., Jiang, H., Stepczynska, A., Wang, C., Buer, J., et al. (2007) · Nature Genetics · doi:10.1038/ng1937 · Cited by 426 · cited 1×
“Analysis of the p21/WAF1 knock-out mice revealed no evidence of spontaneous tumorigenesis in the absence of growth arrest (Choudhury et al., 2007).”
BackgroundMaddocks, O. D. K., & Vousden, K. H. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0735-5 · Cited by 355
Jennis, M., Kung, C.-P., Basu, S., Budina-Kolomets, A., Leu, J. I.-J., Khaku, S., Scott, J. P., Cai, K. Q., Campbell, M. R., Porter, D. K., et al. (2016) · Genes & Development · doi:10.1101/gad.275891.115 · Cited by 352
Cystine-Glutamate Transporter SLC7A11 in Cancer Chemosensitivity and Chemoresistance
Huang, Y., Dai, Z., Barbacioru, C., & Sadée, W. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4267 · Cited by 340
p53 modulation of the DNA damage response
Helton, E. S., & Chen, X. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21091 · Cited by 293
Valente, L. J., Gray, D. H. D., Michalak, E. M., Pinon-Hofbauer, J., Egle, A., Scott, C. L., Janic, A., & Strasser, A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.012 · Cited by 291
Tumor suppressor p53 and its mutants in cancer metabolism
Liu, J., Zhang, C., Hu, W., & Feng, Z. (2015) · Cancer Letters · doi:10.1016/j.canlet.2013.12.025 · Cited by 271
Dynamic roles of p53-mediated metabolic activities in ROS-induced stress responses
Jiang, L., Hickman, J. H., Wang, S.-J., & Gu, W. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1068479 · Cited by 231
Self-citationMichalak, E. M., Villunger, A., Adams, J. M., & Strasser, A. (2008) · Cell Death & Differentiation · doi:10.1038/cdd.2008.16 · Cited by 205
TIGAR Is Required for Efficient Intestinal Regeneration and Tumorigenesis
Cheung, E. C., Athineos, D., Lee, P., Ridgway, R. A., Lambie, W., Nixon, C., Strathdee, D., Blyth, K., Sansom, O. J., & Vousden, K. H. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.001 · Cited by 187
Zhang, Q., Zeng, S. X., Zhang, Y., Zhang, Y.-W., Ding, D., Ye, Q.-Z., Meroueh, S. O., & Lu, H. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201100211 · Cited by 112
The Regulation of Aging and Longevity: A New and Complex Role of p53
Feng, Z., Lin, M., & Wu, R. (2011) · Genes & Cancer · doi:10.1177/1947601911410223 · Cited by 89
The Mdm network and its regulation of p53 activities: a rheostat of cancer risk
Eischen, C. M., & Lozano, G. (2014) · Human Mutation · doi:10.1002/humu.22524 · Cited by 79
To be, or not to be: functional dilemma of p53 metabolic regulation
Wang, S.-J., & Gu, W. J. (2013) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000024 · Cited by 59
Self-citationBiochemical pathways that regulate acetyltransferase and deacetylase activity in mammalian cells
Mellert, H. S., & McMahon, S. B. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.06.010 · Cited by 53
Inauhzin and Nutlin3 synergistically activate p53 and suppress tumor growth
Zhang, Y.-W., Zhang, Q., Zeng, S. X., Zhang, Y., Mayo, L. D., & Lu, H. (2012) · Cancer Biology & Therapy · doi:10.4161/cbt.20844 · Cited by 29
Using Mouse Models to Explore MDM-p53 Signaling in Development, Cell Growth, and Tumorigenesis
Gannon, H., & Jones, S. N. (2012) · Genes & Cancer · doi:10.1177/1947601912455324 · Cited by 25
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.
