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

43 Citations (Scopus)

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

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Pyruvate Kinase
Glycolysis
Oncogenes
Lymphoma
Cells
Phosphorylation
Neoplasms
Protein-Serine-Threonine Kinases
Therapeutics

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Proviral insertion in murine lymphomas 2 (PIM2) oncogene phosphorylates pyruvate kinase M2 (PKM2) and promotes glycolysis in cancer cells. / Yu, Zhenhai; Zhao, Xiaoping; Huang, Liangqian; Zhang, Teng; Yang, Fajun; Xie, Lei; Song, Shaoli; Miao, Ping; Zhao, Li; Sun, Xiaoguang; Liu, Jianjun; Huang, Gang.

In: Journal of Biological Chemistry, Vol. 288, No. 49, 06.12.2013, p. 35406-35416.

Research output: Contribution to journalArticle

Yu, Z, Zhao, X, Huang, L, Zhang, T, Yang, F, Xie, L, Song, S, Miao, P, Zhao, L, Sun, X, Liu, J & Huang, G 2013, 'Proviral insertion in murine lymphomas 2 (PIM2) oncogene phosphorylates pyruvate kinase M2 (PKM2) and promotes glycolysis in cancer cells', Journal of Biological Chemistry, vol. 288, no. 49, pp. 35406-35416. https://doi.org/10.1074/jbc.M113.508226
Yu, Zhenhai ; Zhao, Xiaoping ; Huang, Liangqian ; Zhang, Teng ; Yang, Fajun ; Xie, Lei ; Song, Shaoli ; Miao, Ping ; Zhao, Li ; Sun, Xiaoguang ; Liu, Jianjun ; Huang, Gang. / Proviral insertion in murine lymphomas 2 (PIM2) oncogene phosphorylates pyruvate kinase M2 (PKM2) and promotes glycolysis in cancer cells. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 49. pp. 35406-35416.
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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.",
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AU - Zhao, Xiaoping

AU - Huang, Liangqian

AU - Zhang, Teng

AU - Yang, Fajun

AU - Xie, Lei

AU - Song, Shaoli

AU - Miao, Ping

AU - Zhao, Li

AU - Sun, Xiaoguang

AU - Liu, Jianjun

AU - Huang, Gang

PY - 2013/12/6

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AB - 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.

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