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. 2022 Oct 25;79(11):565. doi: 10.1007/s00018-022-04585-8

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© The Author(s) 2022

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Flux of autophagy protein LC3B-II in wild-type HT-1080 and Gp78 knockout cell lines. Western blot analysis and probing of LC3B-II in HT-1080 cells and g1-4 and g2-41 Gp78 knockout CRISPR/Cas clones after 4 h treatment with either DMSO, CCCP or starvation in presence of 100 nM of BafA1 for 0, 30, 60 and 120 min. DMSO or serum-starved cells show increased and accumulated LC3B-II with BafA1 in time-dependent manner. The slope of LC3B-II band density quantified relative to β-actin show significant differences between the three cell lines; LC3B-II flux upon CCCP treatment of HT-1080 cells but not in the Gp78 knockout clones can be seen (n = 4 independent biological replicates; *, p < 0.05; Mean ± SEM; full blots shown in Supp. Figure 7)