Modification of Drosophila p53 by SUMO Modulates Its Transactivation and Pro-apoptotic Functions
Open accessAbstract
Conjugation to SUMO is a reversible post-translational modification that regulates several transcription factors involved in cell proliferation, differentiation, and disease. The p53 tumor suppressor can be modified by SUMO-1 in mammalian cells, but the functional consequences of this modification are unclear. Here, we demonstrate that the Drosophila homolog of human p53 can be efficiently sumoylated in insect cells. We identify two lysine residues involved in SUMO attachment, one at the C terminus, between the DNA binding and oligomerization domains, and one at the N terminus of the protein. We find that sumoylation helps recruit Drosophila p53 to nuclear dot-like structures that can be marked by human PML and the Drosophila homologue of Daxx. We demonstrate that mutation of both sumoylation sites dramatically reduces the transcriptional activity of p53 and its ability to induce apoptosis in transgenic flies, providing in vivo evidence that sumoylation is critical for Drosophila p53 function.
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Arf can stimulate Mdm2-dependent SUMOylation of itself and of p53 at K386, and SUMOylation is associated with relocalization of p53 to subnuclear structures.
“There is some consensus that Arf can stimulate the Mdm2-dependent SUMOylation of both itself and of p53 at K386 [119,120] and that SUMOylation is associated with relocalization of p53 to subnuclear structures [121,122].”
From The p53 orchestra: Mdm2 and Mdmx set the tone (2010) · cites this paper as [122]
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References 46 · Cited by 33
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- Jin, S., Martinek, S., Joo, W. S., Wortman, J. R., Mirkovic, N., Sali, A., Yandell, M. D., Pavletich, N. P., Young, M. W., and Levine, A. J. (2000) Proc. Natl. Acad. Sci. U. S. A. 97, 7301-7306
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- Peters, M., DeLuca, C., Hirao, A., Stambolic, V., Potter, J., Zhou, L., Liepa, J., Snow, B., Arya, S., Wong, J., Bouchard, D., Binari, R., Manoukian, A. S., and Mak, T. W. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 11305-11310
- Authors
- Mauri, F., McNamee, L. M., Lunardi, A., Chiacchiera, F., Del Sal, G., Brodsky, M. H., & Collavin, L.
- Affiliations
- AREA Science Park (IT)
- University of Massachusetts Chan Medical School (US)
- University of Trieste (IT)
- Corresponding author
- Collavin, Licio
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 283
- Issue
- 30
- Pages
- 20848-20856
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3258953
- OpenAlex
- W2130272450
- Cited by
- 33
- References
- 46
- Citations by year
- 2026: 1 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 4 · 2013: 3 · 2012: 2
- FWCI
- 2.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion)
- Dépôt institutionnel de l'Université libre de Bruxelles (Université Libre de Bruxelles) (submittedVersion, other-oa)
- Iris (University of Trento) (submittedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Keywords
- p53, SUMO1, SUMOylation, post-translational modification, transcriptional activation, apoptosis, lysine modification sites, PML, DAXX, tumor suppressor
- MeSH terms
- Animals, Cell Differentiation, Drosophila, Models, Biological, Mutation, Nuclear Proteins, RNA, Messenger, Transcriptional Activation, Tumor Suppressor Protein p53, Apoptosis, Protein Structure, Tertiary, Small Ubiquitin-Related Modifier Proteins, Animals, Genetically Modified, Adaptor Proteins, Signal Transducing, Cell Proliferation
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