ATG3 proteins possess a unique amphipathic α-helix essential for the Atg8/LC3 lipidation reaction
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- Taki Nishimura
- PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo, Japan
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- Gianmarco Lazzeri
- Frankfurt Institute for Advanced Studies, Frankfurt, Hesse, Germany
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- Sharon A. Tooze
- Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, UK
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- Roberto Covino
- Frankfurt Institute for Advanced Studies, Frankfurt, Hesse, Germany
Description
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.
Journal
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- Autophagy
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Autophagy 20 (1), 212-213, 2023-09-07
Informa UK Limited
