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. 2021 Nov 30;12:6996. doi: 10.1038/s41467-021-27344-y

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© The Author(s) 2021

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. 5 — a Alignment of two putative diacidic ER export motifs (labeled with rectangles) of WFS1 from multiple organisms. Two known pathogenic mutations (E158K and E169K) disrupt these motifs. b In vitro pull-down analysis of the interaction between the WFS1 protein and COPII vesicle subunits. Lysates from HEK-293T cells expressing HA-tagged WFS1 proteins were subjected to pull down with purified Sumo^His-tagged COPII vesicle subunits. IB analysis of pull-down samples showing WFS1 interacts with SEC24A, SEC24B, and SEC24C. n = 3 independent experiments. c Representative imaging of the interaction between WFS1 and COPII vesicle subunits by PLA. The puncta number per cell was quantified by ImageJ software. n = 3 independent experiments, n = 8 independent images quantified. Scale bar, 10 μm. d In vitro pull-down analysis of the interaction between the N-terminal segment of WFS1 protein and COPII vesicle subunits. Purification of recombinant Sumo^His-tagged COPII vesicle subunits was subjected to pull down by the purified recombinant GST-tagged N-terminal segment of WFS1. IB analysis of pull-down samples showing the N-terminal segment of WFS1 interacts with SEC24A, SEC24B and SEC24C. n = 3 independent experiments. e Representative imaging of the interaction between SEC24A and mutant WFS1 proteins by PLA. The puncta number per cell was quantified by ImageJ software. n = 3 independent experiments, n = 8 independent images quantified. Scale bar, 10 μm. f In vitro pull-down analysis of the interaction between mutant WFS1 and the COPII vesicle subunit SEC24A. Lysates from HEK-293T cells expressing HA-tagged mutant WFS1 were subjected to pull down by the purified SEC24A protein. IB analysis of pull-down samples showing only WT WFS1 protein pulled down by SEC24A. n = 3 independent experiments. Molecular weights are in kDa. All the data are presented as mean ± s.e.m. p < 0.05, significant, using a two-tailed Student’s t-test. Source data are provided as a Source Data file.