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Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
Published on: June 16, 2023
A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation
Yi-Tong Li1,2, Cong Yi3, Chen-Chen Chen1
1School of Biological and Medical Engineering, Hefei University of Technology, Anhui, Hefei 230009, China.
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.
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