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. 2020 Jul 3;11:3306. doi: 10.1038/s41467-020-17163-y

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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, b Crystal structures of GABARAP-FAM134B^450–468, GABARAP-SEC62^361–376, and RTN3^245–264. Green and pink indicate GABARAP and ER-phagy receptor AIMs, respectively. c Superimposition of Atg8/GABARAP-binding regions of ER-phagy receptors based on the structures of Atg8 and GABARAP. d, e Binding affinity of FAM134B (d) and SEC62 (e) peptides to GABARAP was measured by ITC.