The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Inhibition of HDM2 and Activation of p53 by Ribosomal Protein L23
Open accessAbstract
The importance of coordinating cell growth with proliferation has been recognized for a long time. The molecular basis of this relationship, however, is poorly understood. Here we show that the ribosomal protein L23 interacts with HDM2. The interaction involves the central acidic domain of HDM2 and an N-terminal domain of L23. L23 and L11, another HDM2-interacting ribosomal protein, can simultaneously yet distinctly interact with HDM2 together to form a ternary complex. We show that, when overexpressed, L23 inhibits HDM2-induced p53 polyubiquitination and degradation and causes a p53-dependent cell cycle arrest. On the other hand, knocking down L23 causes nucleolar stress and triggers translocation of B23 from the nucleolus to the nucleoplasm, leading to stabilization and activation of p53. Our data suggest that cells may maintain a steady-state level of L23 during normal growth; alternating the levels of L23 in response to changing growth conditions could impinge on the HDM2-p53 pathway by interrupting the integrity of the nucleolus.
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Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“The tumor suppressor protein p53 plays a pivotal role in preventing damaged and abnormal cells from becoming malignant, and its loss of function is associated with a majority of human cancers (26, 36 , 37).”
BackgroundMdm2 promotes the rapid degradation of p53
Haupt, Y., Maya, R., Kazaz, A., & Oren, M. (1997) · Nature · doi:10.1038/387296a0 · Cited by 4,506
Regulation of p53 stability by Mdm2
Kubbutat, M. H. G., Jones, S. N., & Vousden, K. H. (1997) · Nature · doi:10.1038/387299a0 · Cited by 3,312 · cited 1×
“This is accomplished by the proto-oncoprotein HDM2 (human counterpart of MDM2 in mice) through either ubiquitin-dependent p53 degradation in the cytoplasm (6, 7, 11) or repression of p53 transcriptional activity in the nucleus (17, 35).”
BackgroundMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
Shieh, S.-Y., Ikeda, M., Taya, Y., & Prives, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80416-x · Cited by 2,100
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
Honda, R., Tanaka, H., & Yasuda, H. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01480-4 · Cited by 1,951
Zhang, Y., Xiong, Y., & Yarbrough, W. G. (1998) · Cell · doi:10.1016/s0092-8674(00)81401-4 · Cited by 1,626
Self-citationA p53 Amino-Terminal Nuclear Export Signal Inhibited by DNA Damage-Induced Phosphorylation
Zhang, Y., & Xiong, Y. (2001) · Science · doi:10.1126/science.1058637 · Cited by 378 · cited 1×
“Indirect immunofluorescence. Indirect immunofluorescence was previously described in detail ( 43 ).”
BackgroundSelf-citation
Cited by
MYC as a regulator of ribosome biogenesis and protein synthesis
van Riggelen, J., Yetil, A., & Felsher, D. W. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2819 · Cited by 956
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
Self-citationGazda, H. T., Sheen, M. R., Vlachos, A., Choesmel, V., O'Donohue, M.-F., Schneider, H., Darras, N., Hasman, C., Sieff, C. A., Newburger, P. E., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.11.004 · Cited by 417
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
MDMX regulation of p53 response to ribosomal stress
Gilkes, D. M., Chen, L., & Chen, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601424 · Cited by 142
Metadata
- Authors
- Jin, A., Itahana, K., O'Keefe, K., & Zhang, Y.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2004-09
- Volume
- 24
- Issue
- 17
- Pages
- 7669-7680
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2142994892
- Cited by
- 353
- References
- 8
- FWCI
- 8.08
- Type
- journal article
- Language
- en
- Open access
- green
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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).
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