Ontology highlight
ABSTRACT:
SUBMITTER: Liang J
PROVIDER: S-EPMC4976202 | biostudies-other | 2016 Aug
REPOSITORIES: biostudies-other
Liang Ji J Cao Ruixiu R Zhang Yajuan Y Xia Yan Y Zheng Yanhua Y Li Xinjian X Wang Liwei L Yang Weiwei W Lu Zhimin Z
Nature communications 20160803
Many types of human tumour cells overexpress the dual-specificity phosphatase Cdc25A. Cdc25A dephosphorylates cyclin-dependent kinase and regulates the cell cycle, but other substrates of Cdc25A and their relevant cellular functions have yet to be identified. We demonstrate here that EGFR activation results in c-Src-mediated Cdc25A phosphorylation at Y59, which interacts with nuclear pyruvate kinase M2 (PKM2). Cdc25A dephosphorylates PKM2 at S37, and promotes PKM2-dependent β-catenin transactiva ...[more]