NDLI: Modification of Drosophila p53 by SUMO modulates its transactivation and pro-apoptotic functions.

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Modification of Drosophila p53 by SUMO modulates its transactivation and pro-apoptotic functions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mcnamee, Laura M. Collavin, Licio Del Sal, Giannino Chiacchiera, Fulvio Brodsky, Michael H. Mauri, Federico Lunardi, Andrea
Description	Author Affiliation: Mauri F ( Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie, AREA Science Park, Padriciano 99, Trieste, Italy.)
Abstract	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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	30
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-07-25
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Drosophila Metabolism RNA, Messenger Transcriptional Activation Adaptor Proteins, Signal Transducing Animals Animals, Genetically Modified Apoptosis Cell Differentiation Cell Proliferation Models, Biological Mutation Nuclear Proteins Protein Structure, Tertiary Small Ubiquitin-Related Modifier Proteins Tumor Suppressor Protein P53 Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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