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

doi:10.1074/jbc.M113.508226

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

Medicine

Research output: Contribution to journal › Article › peer-review

73 Scopus citations

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 language	English (US)
Pages (from-to)	35406-35416
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	49
DOIs	https://doi.org/10.1074/jbc.M113.508226
State	Published - Dec 6 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.508226

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

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.",

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

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doi = "10.1074/jbc.M113.508226",

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TY - JOUR

T1 - Proviral insertion in murine lymphomas 2 (PIM2) oncogene phosphorylates pyruvate kinase M2 (PKM2) and promotes glycolysis in cancer cells

AU - Yu, Zhenhai

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

Y1 - 2013/12/6

N2 - 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.

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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JO - Journal of Biological Chemistry

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IS - 49

ER -

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

Abstract

ASJC Scopus subject areas

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