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. 2022 Jul 21;21:150. doi: 10.1186/s12943-022-01605-w

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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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — MARCKSL1–2 interacts with SUZ12 in LAD cells. a-b ChIP assay detected the changes in histone-H3 acetylation level at miR-200b promoter in SPC-A1/H1299 cells under shMARCKSL1–2 suppression and that in SPC-A1/DTX/H1299/DTX cells upon MARCKSL1–2 overexpression. c RNA pull-down assay followed by mass spectrometry analysis examined the proteins binding with MARCKSL1–2. d RNA pull- down plus Western blot detected the existence of SUZ12 in the pull-down complexes of MARCKSL1–2. e-f RIP assays followed by AGE or RT-qPCR examined the enrichment of MARCKSL1–2 in SUZ12 groups. g-h. RT-qPCR and Western blot detected the influence of MARCKSL1–2 on SUZ12 expression in indicated LAD cells. ^**P < 0.01. n.s.: no significance