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MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Author

Listed:
  • Yu-Lu Cao

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Shuxia Meng

    (California Institute of Technology)

  • Yang Chen

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Jian-Xiong Feng

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Dong-Dong Gu

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Bing Yu

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Yu-Jie Li

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Jin-Yu Yang

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • Shuang Liao

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

  • David C. Chan

    (California Institute of Technology)

  • Song Gao

    (State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center)

Abstract

Crystal structures of engineered human MFN1 in different stages of GTP hydrolysis provide insights into the GTP-induced conformational changes that promote MFN1 dimerization to bring about mitochondrial fusion.

Suggested Citation

  • Yu-Lu Cao & Shuxia Meng & Yang Chen & Jian-Xiong Feng & Dong-Dong Gu & Bing Yu & Yu-Jie Li & Jin-Yu Yang & Shuang Liao & David C. Chan & Song Gao, 2017. "MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion," Nature, Nature, vol. 542(7641), pages 372-376, February.
    • Handle: RePEc:nat:nature:v:542:y:2017:i:7641:d:10.1038_nature21077
    DOI: 10.1038/nature21077
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    Cited by:

    1. Emmanouil Zacharioudakis & Bogos Agianian & Vasantha Kumar MV & Nikolaos Biris & Thomas P. Garner & Inna Rabinovich-Nikitin & Amanda T. Ouchida & Victoria Margulets & Lars Ulrik Nordstrøm & Joel S. Ri, 2022. "Modulating mitofusins to control mitochondrial function and signaling," Nature Communications, Nature, vol. 13(1), pages 1-20, December.
    2. Shuaifeng Li & Shixun Han & Qi Zhang & Yibing Zhu & Haitao Zhang & Junli Wang & Yang Zhao & Jianhui Zhao & Lin Su & Li Li & Dawang Zhou & Cunqi Ye & Xin-Hua Feng & Tingbo Liang & Bin Zhao, 2022. "FUNDC2 promotes liver tumorigenesis by inhibiting MFN1-mediated mitochondrial fusion," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    3. Lucas Gewehr & Benedikt Junglas & Ruven Jilly & Johannes Franz & Wenyu Eva Zhu & Tobias Weidner & Mischa Bonn & Carsten Sachse & Dirk Schneider, 2023. "SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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