The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation
Open accessAbstract
We recently discovered that heat shock causes nucleolin to relocalize from the nucleolus to the nucleoplasm, whereupon it binds replication protein A and inhibits DNA replication initiation. We report that nucleolin mobilization also occurs following exposure to ionizing radiation (IR) and treatment with camptothecin. Mobilization was selective in that another nucleolar marker, upstream binding factor, did not relocalize in response to IR. Nucleolin relocalization was dependent on p53 and stress, the latter initially stimulating nucleolin-p53 complex formation. Nucleolin relocalization and complex formation in vivo were independent of p53 transactivation but required the p53 C-terminal regulatory domain. Nucleolin and p53 also interact directly in vitro, with a similar requirement for p53 domains. These data indicate a novel p53-dependent mechanism in which cell stress mobilizes nucleolin for transient replication inhibition and DNA repair.
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Cites
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
A role for ATR in the DNA damage-induced phosphorylation of p53
Tibbetts, R. S., Brumbaugh, K. M., Williams, J. M., Sarkaria, J. N., Cliby, W. A., Shieh, S.-Y., Taya, Y., Prives, C., & Abraham, R. T. (1999) · Genes & Development · doi:10.1101/gad.13.2.152 · Cited by 1,046
p53 Activates the CD95 (APO-1/Fas) Gene in Response to DNA Damage by Anticancer Drugs
Müller, M., Wilder, S., Bannasch, D., Israeli, D., Lehlbach, K., Li-Weber, M., Friedman, S. L., Galle, P. R., Stremmel, W., Oren, M., et al. (1998) · The Journal of Experimental Medicine · doi:10.1084/jem.188.11.2033 · Cited by 878
DNA damage induces phosphorylation of the amino terminus of p53
Siliciano, J. D., Canman, C. E., Taya, Y., Sakaguchi, K., Appella, E., & Kastan, M. B. (1997) · Genes & Development · doi:10.1101/gad.11.24.3471 · Cited by 818
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641
p53 represses ribosomal gene transcription
Budde, A., & Grummt, I. (1999) · Oncogene · doi:10.1038/sj.onc.1202402 · Cited by 157
Munsch, D., Watanabe-Fukunaga, R., Bourdon, J.-C., Nagata, S., May, E., Yonish-Rouach, E., & Reisdorf, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.3867 · Cited by 131
Cited by
JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., & Pagano, M. (2007) · Nature · doi:10.1038/nature06255 · Cited by 284
DNA damage repair: anytime, anywhere?
Essers, J., Vermeulen, W., & Houtsmuller, A. B. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.03.004 · Cited by 67
C16orf72/HAPSTR1 is a molecular rheostat in an integrated network of stress response pathways
Amici, D. R., Ansel, D. J., Metz, K. A., Smith, R. S., Phoumyvong, C. M., Gayatri, S., Chamera, T., Edwards, S. L., O’Hara, B. P., Srivastava, S., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2111262119 · Cited by 29
Metadata
- Authors
- Daniely, Y., Dimitrova, D. D., & Borowiec, J. A.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2002-08-01
- Volume
- 22
- Issue
- 16
- Pages
- 6014-6022
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W2154070925
- Cited by
- 171
- References
- 7
- FWCI
- 3.02
- Type
- journal article
- Language
- en
- Open access
- green
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- Daniely, Y., Dimitrova, D. D., & Borowiec, J. A. (2002). Stress-Dependent Nucleolin Mobilization Mediated by p53-Nucleolin Complex Formation. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.22.16.6014-6022.2002
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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.
