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Proteomic identification of p53-dependent protein phosphorylation

Abstract

The p53 tumor suppressor regulates transcription of target genes. We have previously analysed the p53-dependent proteome and identified novel protein targets. Here we have examined p53-dependent phosphorylation using two-dimensional gel electrophoresis and staining with the fluorescent phosphoprotein dye Pro-Q Diamond. We report that p53 induces phosphorylation of a subset of proteins including Nm23, DJ-1, ANXA1 and PrxII. Our identification of p53-dependent phosphorylation of specific target proteins reveals new aspects of the p53-dependent cellular response and suggests that such posttranslational modifications may contribute to p53-mediated tumor suppression.

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Acknowledgements

We thank Dr Bengt Fadeel (Karolinska Institutet, Stockholm, Sweden) for the rabbit polyclonal anti-Annexin 1 antibody and for helpful comments. This work was supported by the Swedish Cancer Society, the Cancer Society of Stockholm, the Swedish Medical Research Council (VR) and Karolinska Institutet.

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Correspondence to K G Wiman.

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Supplementary Information accompanies the paper on the Oncogene website (http://www.nature.com/onc).

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Rahman-Roblick, R., Hellman, U., Becker, S. et al. Proteomic identification of p53-dependent protein phosphorylation. Oncogene 27, 4854–4859 (2008). https://doi.org/10.1038/onc.2008.124

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