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. 2021 Apr 14;17(12):4202–4217. doi: 10.1080/15548627.2021.1907516

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© 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 5. — WLS coordinates a multi-protein complex and regulates ER stress response in A549 cells. (A) Wild-type and various deletion mutants of WLS as indicated. (B) Western blot analysis of UPR sensors and CANX-CALR complex expression in anti-GFP immunoprecipitates from wild-type and mutant WLS-transfected A549 cells. Arrow, HSPA5. (C) Western blot analysis of UPR sensors and calcium regulators (ITPR1, RYR1, and ATP2A1) in A549 cells transfected with wild-type or mutant WLS (Arrow, ITPR1). (D) Confocal microscopy imaging of the interaction between WLS and EIF2AK3 in A549 cells transfected with wild-type or WLSΔCT mutants. WLS, green; EIF2AK3, red; and nuclei, blue. (E) Percentage of autophagic A549 cells transfected with wild-type or WLS mutants. (F) Intracellular calcium levels in A549 cells transfected with wild-type or WLS mutants. (G) glycosylation levels as measured by ELISA in A549 cells transfected with wild-type or WLS mutants. Data were generated from three independent experiments for each panel (***, p< 0.001)