Reference: Li YT, et al. (2017) A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation. Nat Commun 8:14846

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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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Journal Article | Research Support, Non-U.S. Gov't
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Li YT, Yi C, Chen CC, Lan H, Pan M, Zhang SJ, Huang YC, Guan CJ, Li YM, Yu L, ... Show all
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