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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

DOI

10.1371/journal.pone.0082022

Type

Journal article

Journal

PLoS One

Publication Date

2013

Volume

8

Keywords

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