Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis.

@article{Li2016MitochondriaTranslocatedPF,
  title={Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis.},
  author={Xinjian Li and Yuhui Jiang and Janet H. Meisenhelder and Weiwei Yang and David H Hawke and Yanhua Zheng and Yan Xia and Kenneth D. Aldape and Jie He and Tony Hunter and Liwei Wang and Zhimin Lu},
  journal={Molecular cell},
  year={2016},
  volume={61 5},
  pages={
          705-719
        }
}
It is unclear how the Warburg effect that exemplifies enhanced glycolysis in the cytosol is coordinated with suppressed mitochondrial pyruvate metabolism. We demonstrate here that hypoxia, EGFR activation, and expression of K-Ras G12V and B-Raf V600E induce mitochondrial translocation of phosphoglycerate kinase 1 (PGK1); this is mediated by ERK-dependent PGK1 S203 phosphorylation and subsequent PIN1-mediated cis-trans isomerization. Mitochondrial PGK1 acts as a protein kinase to phosphorylate… CONTINUE READING
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