Proteomic identification of p53-dependent protein phosphorylation.
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.
Rahman-Roblick
R
R
Department of Oncology-Pathology, Cancer Center Karolinska, Karolinska Institutet, Stockholm, Sweden.
Hellman
U
U
Becker
S
S
Bader
F G
FG
Auer
G
G
Wiman
K G
KG
Roblick
U J
UJ
D017209:Apoptosis / Q000187:drug effects; D002460:Cell Line; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D016685:Mitomycin / Q000494:pharmacology; D010766:Phosphorylation; D040901:Proteomics; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism*
D016159:Tumor Suppressor Protein p53; D016685:Mitomycin