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PKM2 phosphorylates MLC2 and regulates cytokinesis of tumour cells

Author

Listed:
  • Yuhui Jiang

    (The University of Texas MD Anderson Cancer Center)

  • Yugang Wang

    (The University of Texas MD Anderson Cancer Center)

  • Ting Wang

    (Perelman School of Medicine, University of Pennsylvania)

  • David H. Hawke

    (The University of Texas MD Anderson Cancer Center)

  • Yanhua Zheng

    (The University of Texas MD Anderson Cancer Center)

  • Xinjian Li

    (The University of Texas MD Anderson Cancer Center)

  • Qin Zhou

    (The M.O.E. Key Laboratory of Laboratory Medical Diagnostics, College of Laboratory Medicine, Chongqing Medical University)

  • Sadhan Majumder

    (The University of Texas MD Anderson Cancer Center)

  • Erfei Bi

    (Perelman School of Medicine, University of Pennsylvania)

  • David X. Liu

    (Washington State University College of Pharmacy)

  • Suyun Huang

    (The University of Texas MD Anderson Cancer Center)

  • Zhimin Lu

    (The University of Texas MD Anderson Cancer Center
    The University of Texas MD Anderson Cancer Center
    Cancer Biology Program, The University of Texas Graduate School of Biomedical Sciences at Houston)

Abstract

Pyruvate kinase M2 (PKM2) is expressed at high levels during embryonic development and tumour progression and is important for cell growth. However, it is not known whether it directly controls cell division. Here, we found that Aurora B phosphorylates PKM2, but not PKM1, at T45; this phosphorylation is required for PKM2’s localization and interaction with myosin light chain 2 (MLC2) in the contractile ring region of mitotic cells during cytokinesis. PKM2 phosphorylates MLC2 at Y118, which primes the binding of ROCK2 to MLC2 and subsequent ROCK2-dependent MLC2 S15 phosphorylation. PKM2-regulated MLC2 phosphorylation, which is greatly enhanced by EGF stimulation or EGFRvIII, K-Ras G12V and B-Raf V600E mutant expression, plays a pivotal role in cytokinesis, cell proliferation and brain tumour development. These findings underscore the instrumental function of PKM2 in oncogenic EGFR-, K-Ras- and B-Raf-regulated cytokinesis and tumorigenesis.

Suggested Citation

  • Yuhui Jiang & Yugang Wang & Ting Wang & David H. Hawke & Yanhua Zheng & Xinjian Li & Qin Zhou & Sadhan Majumder & Erfei Bi & David X. Liu & Suyun Huang & Zhimin Lu, 2014. "PKM2 phosphorylates MLC2 and regulates cytokinesis of tumour cells," Nature Communications, Nature, vol. 5(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6566
    DOI: 10.1038/ncomms6566
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    Cited by:

    1. Rong-Hsuan Wang & Pin-Ru Chen & Yue-Ting Chen & Yi-Chang Chen & Yu-Hsin Chu & Chia-Chen Chien & Po-Chen Chien & Shao-Yun Lo & Zhong-Liang Wang & Min-Chen Tsou & Ssu-Yu Chen & Guang-Shen Chiu & Wen-Lin, 2024. "Hydrogen sulfide coordinates glucose metabolism switch through destabilizing tetrameric pyruvate kinase M2," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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