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DHHC9-mediated GLUT1 S-palmitoylation promotes glioblastoma glycolysis and tumorigenesis

Author

Listed:
  • Zhenxing Zhang

    (Chinese Academy of Sciences)

  • Xin Li

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Fan Yang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Chao Chen

    (Chinese Academy of Sciences)

  • Ping Liu

    (Chinese Academy of Sciences)

  • Yi Ren

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Pengkai Sun

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Zixiong Wang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yongping You

    (The First Affiliated Hospital of Nanjing Medical University
    Nanjing Medical University)

  • Yi-Xin Zeng

    (Chinese Academy of Sciences
    Sun Yat-Sen University Cancer Center)

  • Xinjian Li

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Glucose transporter GLUT1 is a transmembrane protein responsible for the uptake of glucose into the cells of many tissues through facilitative diffusion. Plasma membrane (PM) localization is essential for glucose uptake by GLUT1. However, the mechanism underlying GLUT1 PM localization remains enigmatic. We find that GLUT1 is palmitoylated at Cys207, and S-palmitoylation is required for maintaining GLUT1 PM localization. Furthermore, we identify DHHC9 as the palmitoyl transferase responsible for this critical posttranslational modification. Knockout of DHHC9 or mutation of GLUT1 Cys207 to serine abrogates palmitoylation and PM distribution of GLUT1, and impairs glycolysis, cell proliferation, and glioblastoma (GBM) tumorigenesis. In addition, DHHC9 expression positively correlates with GLUT1 PM localization in GBM specimens and indicates a poor prognosis in GBM patients. These findings underscore that DHHC9-mediated GLUT1 S-palmitoylation is critical for glucose supply during GBM tumorigenesis.

Suggested Citation

  • Zhenxing Zhang & Xin Li & Fan Yang & Chao Chen & Ping Liu & Yi Ren & Pengkai Sun & Zixiong Wang & Yongping You & Yi-Xin Zeng & Xinjian Li, 2021. "DHHC9-mediated GLUT1 S-palmitoylation promotes glioblastoma glycolysis and tumorigenesis," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26180-4
    DOI: 10.1038/s41467-021-26180-4
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    References listed on IDEAS

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    1. Qin Wu & Wail ba-alawi & Genevieve Deblois & Jennifer Cruickshank & Shili Duan & Evelyne Lima-Fernandes & Jillian Haight & Seyed Ali Madani Tonekaboni & Anne-Marie Fortier & Hellen Kuasne & Trevor D. , 2020. "GLUT1 inhibition blocks growth of RB1-positive triple negative breast cancer," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
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    Cited by:

    1. Huan Zhang & Yan Sun & Zhaokai Wang & Xiaoju Huang & Lu Tang & Ke Jiang & Xin Jin, 2024. "ZDHHC20-mediated S-palmitoylation of YTHDF3 stabilizes MYC mRNA to promote pancreatic cancer progression," Nature Communications, Nature, vol. 15(1), pages 1-21, December.
    2. Chao Chen & Zhenxing Zhang & Caiyun Liu & Bin Wang & Ping Liu & Shu Fang & Fan Yang & Yongping You & Xinjian Li, 2022. "ATF4-dependent fructolysis fuels growth of glioblastoma multiforme," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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