ATG3 proteins possess a unique amphipathic alpha-helix essential for the Atg8/LC3 lipidation reaction

In our recent paper, we uncovered that ATG3 exhibits a large degree of structural dynamics on autophagic membranes to efficiently carry out LC3 lipidation. ATG3 proteins possess an amphipathic alpha-helix (AH) identified by a small number of bulky and hydrophobic residues. This biophysical fingerprint allows for transient membrane association of ATG3 and facilitates its enzymatic reaction. This study will pave the way for a structural and mechanistic understanding of how membrane association of ATG proteins is orchestrated during autophagosome formation.

Automated summary

In our study, we have discovered that ATG3 exhibits dynamic structural changes on autophagic membranes, allowing for efficient LC3 lipidation. The presence of an amphipathic alpha-helix with bulky and hydrophobic residues enables transient membrane association and facilitates enzymatic reaction of ATG3. This research provides insights into the understanding of how ATG proteins interact with membranes during autophagosome formation.