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Proviral insertion in murine lymphomas 2 (PIM2) oncogene phosphorylates pyruvate kinase M2 (PKM2) and promotes glycolysis in cancer cells

  • Zhenhai Yu
  • , Xiaoping Zhao
  • , Liangqian Huang
  • , Teng Zhang
  • , Fajun Yang
  • , Lei Xie
  • , Shaoli Song
  • , Ping Miao
  • , Li Zhao
  • , Xiaoguang Sun
  • , Jianjun Liu
  • , Gang Huang

Research output: Contribution to journalArticlepeer-review

Abstract

Background: The protein-serine/threonine kinase PIM2 regulates glycolysis, but the mechanism is not fully elucidated. Results: PIM2 interacts with PKM2 and phosphorylates PKM2 on the Thr-454 residue. Conclusion: This phosphorylation of PKM2 increases glycolysis and proliferation in cancer cells. Significance: PIM2-dependent phosphorylation of PKM2 is critical for regulating the Warburg effect in cancer, highlighting PIM2 as a potential therapeutic target.

Original languageEnglish (US)
Pages (from-to)35406-35416
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number49
DOIs
StatePublished - Dec 6 2013

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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