ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect

Pyruvate kinase M2 (PKM2) is upregulated in multiple cancer types and contributes to the Warburg effect by unclarified mechanisms. Here we demonstrate that EGFR-activated ERK2 binds directly to PKM2 I429/L431 via the ERK2 docking groove and phosphorylates PKM2 Ser37 but not PKM1. Phosphorylated PKM2...

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Bibliografische gegevens
Hoofdauteurs: Yang, Weiwei, Zheng, Yanhua, Xia, Yan, Ji, Haitao, Chen, Xiaomin, Guo, Fang, Lyssiotis, Costas A., Aldape, Kenneth, Cantley, Lewis C., Lu, Zhimin
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2012
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Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC3511602/
https://ncbi.nlm.nih.gov/pubmed/23178880
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncb2629
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