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A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation

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  • Yi-Tong Li

    (School of Biological and Medical Engineering, Hefei University of Technology
    Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University)

  • Cong Yi

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Chen-Chen Chen

    (School of Biological and Medical Engineering, Hefei University of Technology)

  • Huan Lan

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University)

  • Man Pan

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University)

  • Shao-Jin Zhang

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Yi-Chao Huang

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University)

  • Chao-Jian Guan

    (School of Biological and Medical Engineering, Hefei University of Technology)

  • Yi-Ming Li

    (School of Biological and Medical Engineering, Hefei University of Technology)

  • Li Yu

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Biomembrane and Membrane Biotechnology, Center for Life Sciences, School of Life Sciences, Tsinghua University)

  • Lei Liu

    (Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology (Ministry of Education), Tsinghua University)

Abstract

Acetylation of Atg3 regulates the lipidation of the protein Atg8 in autophagy. The molecular mechanism behind this important biochemical event remains to be elucidated. We describe the first semi-synthesis of homogeneous K19/K48-diacetylated Atg3 through sequential hydrazide-based native chemical ligation. In vitro reconstitution experiments with the semi-synthetic proteins confirm that Atg3 acetylation can promote the lipidation of Atg8. We find that acetylation of Atg3 enhances its binding to phosphatidylethanolamine-containing liposomes and to endoplasmic reticulum, through which it promotes the lipidation process.

Suggested Citation

  • Yi-Tong Li & Cong Yi & Chen-Chen Chen & Huan Lan & Man Pan & Shao-Jin Zhang & Yi-Chao Huang & Chao-Jian Guan & Yi-Ming Li & Li Yu & Lei Liu, 2017. "A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14846
    DOI: 10.1038/ncomms14846
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