The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis
Open accessAbstract
SUMMARY 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 pyruvate dehydrogenase kinase 1 (PDHK1) at T338, which activates PDHK1 to phosphorylate and inhibit the pyruvate dehydrogenase (PDH) complex. This reduces mitochondrial pyruvate utilization, suppresses reactive oxygen species production, increases lactate production, and promotes brain tumorigenesis. Furthermore, PGK1 S203 and PDHK1 T338 phosphorylation levels correlate with PDH S293 inactivating phosphorylation levels and poor prognosis in glioblastoma patients. This work highlights that PGK1 act as a protein kinase in coordinating glycolysis and the TCA cycle, which is instrumental in cancer metabolism and tumorigenesis.
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Cites
Why Do Cancers Have High Aerobic Glycolysis?
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Nuclear PKM2 regulates β-catenin transactivation upon EGFR activation
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Self-citationERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect
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Self-citationGlucose Deprivation Contributes to the Development of KRAS Pathway Mutations in Tumor Cells
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PKM2 Phosphorylates Histone H3 and Promotes Gene Transcription and Tumorigenesis
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Self-citationPyruvate Kinase M2 Regulates Gene Transcription by Acting as a Protein Kinase
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Vyas, S., Zaganjor, E., & Haigis, M. C. (2016) · Cell · doi:10.1016/j.cell.2016.07.002 · Cited by 1,735
Lactate metabolism in human health and disease
Li, X., Yang, Y., Zhang, B., Lin, X., Fu, X., An, Y., Zou, Y., Wang, J.-X., Wang, Z., & Yu, T. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01151-3 · Cited by 1,454
Self-citationTumor glycolysis, an essential sweet tooth of tumor cells
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Aerobic glycolysis promotes tumor immune evasion by hexokinase2-mediated phosphorylation of IκBα
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Self-citationWang, S., Zheng, Y., Yang, F., Zhu, L., Zhu, X.-Q., Wang, Z.-F., Wu, X.-L., Zhou, C.-H., Yan, J.-Y., Hu, B.-Y., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00659-4 · Cited by 369
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Metadata
- Authors
- Li, X., Jiang, Y., Meisenhelder, J., Yang, W., Hawke, D. H., Zheng, Y., Xia, Y., Aldape, K., He, J., Hunter, T., Wang, L., & Lu, Z.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 61
- Issue
- 5
- Pages
- 705-719
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2292259030
- Cited by
- 508
- References
- 41
- FWCI
- 12.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Li, X., Jiang, Y., Meisenhelder, J., Yang, W., Hawke, D. H., Zheng, Y., Xia, Y., Aldape, K., He, J., Hunter, T., Wang, L., & Lu, Z. (2016). Mitochondria-Translocated PGK1 Functions as a Protein Kinase to Coordinate Glycolysis and the TCA Cycle in Tumorigenesis. Molecular Cell. https://doi.org/10.1016/j.molcel.2016.02.009
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