A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28327644.
- Also identified by DOI 10.1038/ncomms14846 and PMC identifier 5473643.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Autophagy-Related Protein 8 Family
- Autophagy-Related Proteins
- Intracellular Membranes
- Lipids
- Saccharomyces cerevisiae Proteins
- Ubiquitin-Conjugating Enzymes