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We reported recently that apoptosis-stimulating protein of p53 (ASPP) 2, an activator of p53, co-operates with oncogenic RAS to enhance the transcription and apoptotic function of p53. However, the detailed mechanism remains unknown. Here we show that ASPP2 is a novel substrate of mitogen-activated protein kinase (MAPK). Phosphorylation of ASPP2 by MAPK is required for RAS-induced increased binding to p53 and increased transactivation of pro-apoptotic genes. In contrast, an ASPP2 phosphorylation mutant exhibits reduced p53 binding and fails to enhance transactivation and apoptosis. Thus phosphorylation of ASPP2 by RAS/MAPK pathway provides a novel link between RAS and p53 in regulating apoptosis.

Original publication




Journal article


PLoS One

Publication Date





Amino Acid Sequence, Apoptosis, Apoptosis Regulatory Proteins, Cell Line, Tumor, Humans, MAP Kinase Signaling System, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Phosphorylation, Protein Transport, Tumor Suppressor Protein p53, ras Proteins