The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Ribosomal protein S14 unties the MDM2–p53 loop upon ribosomal stress
Open accessAbstract
The MDM2–p53 feedback loop is crucially important for restricting p53 level and activity during normal cell growth and proliferation, and is thus subjected to dynamic regulation in order for cells to activate p53 upon various stress signals. Several ribosomal proteins, such as RPL11, RPL5, RPL23, RPL26 or RPS7, have been shown to have a role in regulation of this feedback loop in response to ribosomal stress. Here, we identify another ribosomal protein S14, which is highly associated with 5q-syndrome, as a novel activator of p53 by inhibiting MDM2 activity. We found that RPS14, but not RPS19, binds to the central acidic domain of MDM2, similar to RPL5 and RPL23, and inhibits its E3 ubiquitin ligase activity toward p53. This RPS14–MDM2 binding was induced upon ribosomal stress caused by actinomycin D or mycophenolic acid. Overexpression of RPS14, but not RPS19, elevated p53 level and activity, leading to G1 or G2 arrest. Conversely, knockdown of RPS14 alleviated p53 induction by these two reagents. Interestingly, knockdown of either RPS14 or RPS19 caused a ribosomal stress that led to p53 activation, which was impaired by further knocking down the level of RPL11 or RPL5. Together, our results demonstrate that RPS14 and RPS19 have distinct roles in regulating the MDM2–p53 feedback loop in response to ribosomal stress.
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Cites
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Mdm2 promotes the rapid degradation of p53
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Cited by
Ribosomal proteins: functions beyond the ribosome
Zhou, X., Liao, W.-J., Liao, J.-M., Liao, P., & Lu, H. (2015) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjv014 · Cited by 743
Self-citationThe MDM2-p53 pathway revisited
Subhasree, N., Jiangjiang, Q., Kalkunte, S., Minghai, W., & Ruiwen, Z. (2013) · The Journal of Biomedical Research · doi:10.7555/jbr.27.20130030 · Cited by 414
Lessard, F., Igelmann, S., Trahan, C., Huot, G., Saint-Germain, E., Mignacca, L., Del Toro, N., Lopes-Paciencia, S., Le Calvé, B., Montero, M., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0127-y · Cited by 174
The role of ubiquitin modification in the regulation of p53
Hock, A. K., & Vousden, K. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.05.022 · Cited by 168
SURF2 is a MDM2 antagonist in triggering the nucleolar stress response
Tagnères, S., Santo, P. E., Radermecker, J., Rinaldi, D., Froment, C., Provost, Q., Bongers, M., Capeille, S., Watkins, N., Marcoux, J., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52659-x · Cited by 15
Metadata
- Authors
- Zhou, X., Hao, Q., Liao, J., Zhang, Q., & Lu, H.
- Venue
- Oncogene
- Published
- 2012-03-05
- Volume
- 32
- Issue
- 3
- Pages
- 388-396
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- OpenAlex
- W1980473722
- Cited by
- 176
- References
- 10
- FWCI
- 7.39
- Type
- journal article
- Language
- en
- Open access
- green
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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.
