Phosphorylation of ASPP2 by RAS/MAPK pathway is critical for its full pro-apoptotic function.
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ABSTRACT:
SUBMITTER: Godin-Heymann N
PROVIDER: S-EPMC3847091 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Publications
Phosphorylation of ASPP2 by RAS/MAPK pathway is critical for its full pro-apoptotic function.
Godin-Heymann Nadia N Wang Yihua Y Slee Elizabeth E Lu Xin X
PloS one 20131202 12
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 ...[more]
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