The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Mdm2 Regulates p53 mRNA Translation through Inhibitory Interactions with Ribosomal Protein L26
Open accessAbstract
Summary Mdm2 regulates the p53 tumor suppressor by promoting its proteasome-mediated degradation. Mdm2 and p53 engage in an autoregulatory feedback loop that maintains low p53 activity in non-stressed cells. We now report that Mdm2 regulates p53 levels also by targeting ribosomal protein L26. L26 binds p53 mRNA and augments its translation. Mdm2 binds L26 and drives its polyubiquitylation and proteasomal degradation. In addition, the binding of Mdm2 to L26 attenuates the association of L26 with p53 mRNA and represses L26-mediated augmentation of p53 protein synthesis. Under non-stressed conditions, both mechanisms help maintain low cellular p53 levels by constitutively tuning down p53 translation. In response to genotoxic stress the inhibitory effect of Mdm2 on L26 is attenuated, enabling a rapid increase in p53 synthesis. The Mdm2-L26 interaction thus represents an additional important component of the autoregulatory feedback loop that dictates cellular p53 levels and activity.
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Citations
Cites
Mdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Self-citationRegulation of p53 stability by Mdm2
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“Furthermore, as a p53-selective E3-ubiquitin ligase, Mdm2 promotes p53 polyubiquitylation and targets p53 to degradation by the 26S proteasome (Fang et al., 2000; Haupt et al., 1997; Honda et al., 1997; Kubbutat et al., 1997).”
BackgroundThe p53 pathway: positive and negative feedback loops
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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
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Amplification of a gene encoding a p53-associated protein in human sarcomas
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ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage
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“It is conceivable that IR-induced modifications of Mdm2 (Blattner et al., 2002; Maya et al., 2001) may not only alter the impact of Mdm2 on p53 but also reduce the ability of Mdm2 to interfere with the binding of L26 to p53 mRNA.”
BackgroundSelf-citationAnalysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
Lam, Y. W., Lamond, A. I., Mann, M., & Andersen, J. S. (2007) · Current Biology · doi:10.1016/j.cub.2007.03.064 · Cited by 369
Keeping p53 in check: essential and synergistic functions of Mdm2 and Mdm4
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Cited by
Boulon, S., Westman, B. J., Hutten, S., Boisvert, F.-M., & Lamond, A. I. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.024 · Cited by 1,103
Signaling to p53: ribosomal proteins find their way
Zhang, Y., & Lu, H. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.09.024 · Cited by 591
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
p53 and E2f: partners in life and death
Polager, S., & Ginsberg, D. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2718 · Cited by 498
The Mdm2–p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
Manfredi, J. J. (2010) · Genes & Development · doi:10.1101/gad.1941710 · Cited by 344
Metadata
- Authors
- Ofir-Rosenfeld, Y., Boggs, K., Michael, D., Kastan, M. B., & Oren, M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 32
- Issue
- 2
- Pages
- 180-189
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2075213054
- Cited by
- 239
- References
- 13
- FWCI
- 11.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Ofir-Rosenfeld, Y., Boggs, K., Michael, D., Kastan, M. B., & Oren, M. (2008). Mdm2 Regulates p53 mRNA Translation through Inhibitory Interactions with Ribosomal Protein L26. Molecular Cell. https://doi.org/10.1016/j.molcel.2008.08.031
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