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. 2020 Jul 31;10:12956. doi: 10.1038/s41598-020-69637-0

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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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Effects of Rab33B and Atg16 mutations on complex formation analyzed by GFP co-immunoprecipitation and Ni-sepharose pulldown experiments. (a) GFP Co-immunoprecipitation. Overexpression was done in HEK293 cells. Western blots were probed with either anti-GFP, anti-V5 or anti-LC3B antibodies. IP immunoprecipitation. (b) Quantification of the western blot band intensities shown in (a). Band intensities were calculated by normalizing the V5-IP blot band intensities against GFP-IP intensity. Error bars represent standard errors (SE) of three independent biological replicates. (c) His-Rab33B(30–202) mutants were co-expressed with Atg16L1(153–210) wild-type and mutants. Samples were run on Schägger gels after elution from the Ni-Sepharose beads and then blotted onto nitrocellulose membranes. Membranes were probed with rabbit anti-Atg16L primary antibody and goat anti-rabbit IgG (HRP labeled) secondary antibody. Uncropped images of blots are shown in Figures S7 and S8.