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A Semisynthetic Atg3 Reveals That Acetylation Promotes Atg3 Membrane Binding and Atg8 Lipidation

Overview
Journal Nat Commun
Specialty Biology
Date 2017 Mar 23
PMID 28327644
Citations 24
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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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