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 journalArticle

45 Scopus citations


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
Issue number49
StatePublished - Dec 6 2013


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this