Back to Search
Start Over
A semisynthetic Atg3 reveals that acetylation promotes Atg3 membrane binding and Atg8 lipidation
- Source :
- Nature Communications, Vol 8, Iss 1, Pp 1-9 (2017), Nature Communications
- Publication Year :
- 2017
- Publisher :
- Nature Portfolio, 2017.
-
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.<br />Acetylation of Atg3 regulates lipidation of Atg8 and therefore autophagy, but the molecular mechanisms remain unclear. Here, Li et al. semi-synthesize diacetylated Atg3, allowing them to show that acetylated Atg3 enhances Atg8 lipidation by promoting interaction of Atg3 with liposomes containing physiological levels of phosphatidylethanolamine.
- Subjects :
- 0301 basic medicine
Saccharomyces cerevisiae Proteins
ATG8
Science
Lysine
General Physics and Astronomy
Autophagy-Related Proteins
Lipid-anchored protein
Plasma protein binding
Saccharomyces cerevisiae
Ubiquitin-conjugating enzyme
Endoplasmic Reticulum
Models, Biological
General Biochemistry, Genetics and Molecular Biology
Article
03 medical and health sciences
Amino Acid Sequence
Multidisciplinary
Chemistry
Endoplasmic reticulum
Acetylation
Esters
General Chemistry
Autophagy-Related Protein 8 Family
Intracellular Membranes
Native chemical ligation
Lipids
Cell biology
030104 developmental biology
Liposomes
Ubiquitin-Conjugating Enzymes
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 8
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....112450e16ed9eb50afcfa780139774c1