Proteomic identification of p53-dependent protein phosphorylation

• Published in: Oncogene Vol. 27; no. 35; pp. 4854 - 4859
• Main Authors: Rahman-Roblick, R, Hellman, U, Becker, S, Bader, F G, Auer, G, Wiman, K G, Roblick, U J
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 14.08.2008; Nature Publishing; Nature Publishing Group
• Subjects: Apoptosis; Apoptosis - drug effects; Biological and medical sciences; Cancer; Cell Biology; Cell Line; Cell physiology; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes; Cellular biology; Diverse techniques; Electrophoresis, Gel, Two-Dimensional; Fundamental and applied biological sciences. Psychology; Gel electrophoresis; Health aspects; Human Genetics; Humans; Identification and classification; Internal Medicine; Kinases; MEDICIN; Medicin och hälsovetenskap; MEDICINE; Medicine & Public Health; Mitomycin - pharmacology; Molecular and cellular biology; Nucleoside-diphosphate kinase; Oncology; p53; p53 Protein; PARK7 protein; Phosphorylation; Properties; Proteins; Proteomes; Proteomics; short-communication; Transcription; Tumor suppressor genes; Tumor Suppressor Protein p53 - metabolism; Tumors; Sweden; proteomics; phosphorylation; p53; Phosphorylation; TP53 Gene; p53 Protein; Proteomics; Identification; Carcinogenesis; Tumor suppressor gene
• ISSN: 0950-9232; 1476-5594; 1476-5594
• DOI: 10.1038/onc.2008.124

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.