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. 2020 May 26;6:32. doi: 10.1038/s41421-020-0161-3

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — a The lipidation system of LC3. ATG4 cleaves the C-terminal residues of LC3 to expose glycine (G) residue. Then, LC3 is activated by ATG7 (E1 enzyme) and transferred to ATG3 (E2 enzyme). ATG12–5-16L1 complex facilitates the transfer of LC3 from ATG3 to PE. A PI3P-binding protein WIPI2B controls membrane recruitment of ATG12–5-16L1 complex under starvation condition. b The domain structures of H. sapiens ATG16L1 and S. cerevisiae Atg16 proteins. c The domain structures of H. sapiens ATG3 and S. cerevisiae Atg3 proteins. CC coiled-coil, AH amphipathic helix, FR flexible region, HR handle region, AIM Atg8 family-interacting motif.