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. 2021 Aug 3;40(39):5829–5842. doi: 10.1038/s41388-021-01877-4

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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. 8 — A Immunoprecipitation (IP) was conducted using KRAS antibody (rabbit derived) and followed by Western blot using LYPLA1 antibody (rabbit derived). B IP using LYPLA1 antibody and followed by Western blot using KRAS antibody. C IP using RNF141 antibody and followed by Western blot using LYPLA1 antibody. D IP using LYPLA1 antibody and followed by Western blot using RNF141 antibody. IgG antibody (rabbit or mouse derived) was used as non-specific control. E IF assay displayed the level of KRAS on the membrane after treatment with palmostatin B (50 μΜ, incubation 6 h) in HCT116 cells transfected with LV-NC and LV-RNF141. Scale bar, 20 μm. F, G Western blot analyses for KRAS downstream effectors (F) and PCNA and apoptotic markers (G) after treatment with palmostatin B (50 μΜ, incubation 6 h) in HCT116 cells transfected with LV-NC and LV-RNF141. Bar graphs were presented as the mean ± SD from three independent experiments. **P < 0.01, ***P < 0.001. n.s. represents no significance.