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

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 () and Lei Liu ()
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Yi-Tong Li: School of Biological and Medical Engineering, Hefei University of Technology
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

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: 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.

Date: 2017
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DOI: 10.1038/ncomms14846

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