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DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe

Author

Listed:
  • Qi Liu

    (Chinese Academy of Sciences
    Shandong University)

  • Qing-tao He

    (Chinese Academy of Sciences
    Shandong University
    Peking University)

  • Xiaoxuan Lyu

    (Chinese Academy of Sciences)

  • Fan Yang

    (Shandong University
    Peking University)

  • Zhong-liang Zhu

    (University of Science and Technology of China)

  • Peng Xiao

    (Shandong University
    Peking University)

  • Zhao Yang

    (Shandong University
    Peking University)

  • Feng Zhang

    (Chinese Academy of Sciences)

  • Zhao-ya Yang

    (Chinese Academy of Sciences
    Shandong University)

  • Xiao-yan Wang

    (Chinese Academy of Sciences)

  • Peng Sun

    (Chinese Academy of Sciences)

  • Qian-wen Wang

    (Chinese Academy of Sciences)

  • Chang-xiu Qu

    (Shandong University
    Peking University)

  • Zheng Gong

    (Shandong University)

  • Jing-yu Lin

    (Shandong University)

  • Zhen Xu

    (Chinese Academy of Sciences)

  • Shao-le Song

    (Chinese Academy of Sciences)

  • Shen-ming Huang

    (Peking University)

  • Sheng-chao Guo

    (Shandong University
    Peking University)

  • Ming-jie Han

    (Chinese Academy of Sciences
    Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences)

  • Kong-kai Zhu

    (University of Jinan)

  • Xin Chen

    (Changzhou University)

  • Alem W. Kahsai

    (Duke University, School of Medicine)

  • Kun-Hong Xiao

    (University of Pittsburgh)

  • Wei Kong

    (Peking University)

  • Fa-hui Li

    (Chinese Academy of Sciences)

  • Ke Ruan

    (University of Science and Technology of China)

  • Zi-jian Li

    (Peking University)

  • Xiao Yu

    (Shandong University)

  • Xiao-gang Niu

    (Peking University)

  • Chang-wen Jin

    (Peking University)

  • Jiangyun Wang

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

  • Jin-peng Sun

    (Shandong University
    Peking University)

Abstract

Characterization of the dynamic conformational changes in membrane protein signaling complexes by nuclear magnetic resonance (NMR) spectroscopy remains challenging. Here we report the site-specific incorporation of 4-trimethylsilyl phenylalanine (TMSiPhe) into proteins, through genetic code expansion. Crystallographic analysis revealed structural changes that reshaped the TMSiPhe-specific amino-acyl tRNA synthetase active site to selectively accommodate the trimethylsilyl (TMSi) group. The unique up-field 1H-NMR chemical shift and the highly efficient incorporation of TMSiPhe enabled the characterization of multiple conformational states of a phospho-β2 adrenergic receptor/β-arrestin-1(β-arr1) membrane protein signaling complex, using only 5 μM protein and 20 min of spectrum accumulation time. We further showed that extracellular ligands induced conformational changes located in the polar core or ERK interaction site of β-arr1 via direct receptor transmembrane core interactions. These observations provided direct delineation and key mechanism insights that multiple receptor ligands were able to induce distinct functionally relevant conformational changes of arrestin.

Suggested Citation

  • Qi Liu & Qing-tao He & Xiaoxuan Lyu & Fan Yang & Zhong-liang Zhu & Peng Xiao & Zhao Yang & Feng Zhang & Zhao-ya Yang & Xiao-yan Wang & Peng Sun & Qian-wen Wang & Chang-xiu Qu & Zheng Gong & Jing-yu Li, 2020. "DeSiphering receptor core-induced and ligand-dependent conformational changes in arrestin via genetic encoded trimethylsilyl 1H-NMR probe," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18433-5
    DOI: 10.1038/s41467-020-18433-5
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    Citations

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    Cited by:

    1. Yutaro Shiraishi & Yutaka Kofuku & Takumi Ueda & Shubhi Pandey & Hemlata Dwivedi-Agnihotri & Arun K. Shukla & Ichio Shimada, 2021. "Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    2. Ruibo Zhai & Zhuoqi Wang & Zhaofei Chai & Xiaogang Niu & Conggang Li & Changwen Jin & Yunfei Hu, 2023. "Distinct activation mechanisms of β-arrestin-1 revealed by 19F NMR spectroscopy," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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