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MAVS integrates glucose metabolism and RIG-I-like receptor signaling

Author

Listed:
  • Qiao-qiao He

    (Wuhan University)

  • Yu Huang

    (Wuhan University)

  • Longyu Nie

    (Wuhan University)

  • Sheng Ren

    (Wuhan University)

  • Gang Xu

    (Wuhan University)

  • Feiyan Deng

    (Wuhan University)

  • Zhikui Cheng

    (Wuhan University)

  • Qi Zuo

    (Wuhan University)

  • Lin Zhang

    (Wuhan University
    Zhongnan Hospital of Wuhan University)

  • Huanhuan Cai

    (Wuhan University
    Zhongnan Hospital of Wuhan University)

  • Qiming Wang

    (Hunan Agricultural University)

  • Fubing Wang

    (Chinese Academy of Medical Sciences)

  • Hong Ren

    (Affiliated Hospital to Shanghai Jiao Tong University School of Medicine)

  • Huan Yan

    (Wuhan University)

  • Ke Xu

    (Wuhan University)

  • Li Zhou

    (Wuhan University)

  • Mengji Lu

    (University Hospital Essen, University of Duisburg-Essen)

  • Zhibing Lu

    (Wuhan University
    Zhongnan Hospital of Wuhan University)

  • Ying Zhu

    (Wuhan University)

  • Shi Liu

    (Wuhan University
    Wuhan University
    Hunan Agricultural University
    Chinese Academy of Medical Sciences)

Abstract

MAVS is an adapter protein involved in RIG-I-like receptor (RLR) signaling in mitochondria, peroxisomes, and mitochondria-associated ER membranes (MAMs). However, the role of MAVS in glucose metabolism and RLR signaling cross-regulation and how these signaling pathways are coordinated among these organelles have not been defined. This study reports that RLR action drives a switch from glycolysis to the pentose phosphate pathway (PPP) and the hexosamine biosynthesis pathway (HBP) through MAVS. We show that peroxisomal MAVS is responsible for glucose flux shift into PPP and type III interferon (IFN) expression, whereas MAMs-located MAVS is responsible for glucose flux shift into HBP and type I IFN expression. Mechanistically, peroxisomal MAVS interacts with G6PD and the MAVS signalosome forms at peroxisomes by recruiting TNF receptor-associated factor 6 (TRAF6) and interferon regulatory factor 1 (IRF1). By contrast, MAMs-located MAVS interact with glutamine-fructose-6-phosphate transaminase, and the MAVS signalosome forms at MAMs by recruiting TRAF6 and TRAF2. Our findings suggest that MAVS mediates the interaction of RLR signaling and glucose metabolism.

Suggested Citation

  • Qiao-qiao He & Yu Huang & Longyu Nie & Sheng Ren & Gang Xu & Feiyan Deng & Zhikui Cheng & Qi Zuo & Lin Zhang & Huanhuan Cai & Qiming Wang & Fubing Wang & Hong Ren & Huan Yan & Ke Xu & Li Zhou & Mengji, 2023. "MAVS integrates glucose metabolism and RIG-I-like receptor signaling," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41028-9
    DOI: 10.1038/s41467-023-41028-9
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    1. Dara L. Burdette & Kathryn M. Monroe & Katia Sotelo-Troha & Jeff S. Iwig & Barbara Eckert & Mamoru Hyodo & Yoshihiro Hayakawa & Russell E. Vance, 2011. "STING is a direct innate immune sensor of cyclic di-GMP," Nature, Nature, vol. 478(7370), pages 515-518, October.
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