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• W4384697935 abstract "Abstract The covalent attachment of ubiquitin-like LC3 proteins prepares the autophagic membrane for cargo recruitment. We resolve key steps in LC3 lipidation by combining molecular dynamics simulations and experiments in vitro and in cellulo . We show how the E3-like ligase ATG12– ATG5-ATG16L1 in complex with the E2-like conjugase ATG3 docks LC3 onto the membrane in three steps by (1) the PI(3)P effector protein WIPI2, (2) helix α2 of ATG16L1, and (3) a membrane-interacting surface of ATG3. Phosphatidylethanolamine (PE) lipids concentrate in a region around the thioester bond between ATG3 and LC3, highlighting residues with a possible role in the catalytic transfer of LC3 to PE, including two conserved histidines. In a near-complete pathway from the initial membrane recruitment to the LC3 lipidation reaction, the three-step targeting of the ATG12–ATG5-ATG16L1 machinery establishes a high level of regulatory control." @default.
• W4384697935 created "2023-07-20" @default.
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• W4384697935 date "2023-07-17" @default.
• W4384697935 modified "2023-10-06" @default.
• W4384697935 title "Three-step docking by WIPI2, ATG16L1 and ATG3 delivers LC3 to the phagophore" @default.
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• W4384697935 doi "https://doi.org/10.1101/2023.07.17.549391" @default.
• W4384697935 hasPublicationYear "2023" @default.
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