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Updated: Jul 17, 2025

Author Spotlight: Imaging ATG9A, a Multi-Spanning Membrane Protein
Published on: June 16, 2023
ATG3 proteins possess a unique amphipathic α-helix essential for the Atg8/LC3 lipidation reaction
Taki Nishimura1,2,3, Gianmarco Lazzeri4,5, Sharon A Tooze3
1PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo, Japan.
Abstract:
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 α-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.
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