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Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1

Author

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  • Jianxiu Zhang

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

  • Ying-Ying Wang

    (Beijing Normal University
    National Institute of Biological Sciences
    Henan University of Science and Technology)

  • Zhao-Qian Pan

    (National Institute of Biological Sciences)

  • Yulu Li

    (National Institute of Biological Sciences)

  • Jianhua Sui

    (National Institute of Biological Sciences
    Tsinghua University)

  • Li-Lin Du

    (National Institute of Biological Sciences
    Tsinghua University)

  • Keqiong Ye

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

Abstract

Neighbor of BRCA1 (Nbr1) is a conserved autophagy receptor that provides cargo selectivity to autophagy. The four-tryptophan (FW) domain is a signature domain of Nbr1, but its exact function remains unclear. Here, we show that Nbr1 from the filamentous fungus Chaetomium thermophilum uses its FW domain to bind the α-mannosidase Ams1, a cargo of selective autophagy in both budding yeast and fission yeast, and delivers Ams1 to the vacuole by conventional autophagy in heterologous fission yeast. The structure of the Ams1-FW complex was determined at 2.2 Å resolution by cryo-electron microscopy. The FW domain adopts an immunoglobulin-like β-sandwich structure and recognizes the quaternary structure of the Ams1 tetramer. Notably, the N-terminal di-glycine of Ams1 is specifically recognized by a conserved pocket of the FW domain. The FW domain becomes degenerated in fission yeast Nbr1, which binds Ams1 with a ZZ domain instead. Our findings illustrate the protein binding mode of the FW domain and reveal the versatility of Nbr1-mediated cargo recognition.

Suggested Citation

  • Jianxiu Zhang & Ying-Ying Wang & Zhao-Qian Pan & Yulu Li & Jianhua Sui & Li-Lin Du & Keqiong Ye, 2022. "Structural mechanism of protein recognition by the FW domain of autophagy receptor Nbr1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-31439-5
    DOI: 10.1038/s41467-022-31439-5
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    1. Do Hoon Kwon & Ok Hyun Park & Leehyeon Kim & Yang Ouk Jung & Yeonkyoung Park & Hyeongseop Jeong & Jaekyung Hyun & Yoon Ki Kim & Hyun Kyu Song, 2018. "Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
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