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. 2022 Mar 12;21:74. doi: 10.1186/s12943-022-01555-3

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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. 3 — hnRNPA2B1 is a direct and functional binding partner of MIR100HG. a Venn diagram proteins identified by mass spectrometry and retrieved by different groups of MIR100HG probes in ChIRP assays. “Even” and “odd” indicate the two groups of biotin-labeled oilgo probe sets designed for MIR100HG. Immunoblots of hnRNPA2B1 enriched by MIR100HG probes in CC-CR and HCT116 cells (bottom right). b RIP assays detecting MIR100HG retrieved by a hnRNPA2B1 specific antibody or by normal IgG. U1 RNA served as a negative control. Inset depicts immunoblots showing pull-down efficiency. n = 3 independent biological replicates. c Graphic illustration of the predicted secondary structure of MIR100HG. d Top: agarose gel electrophoresis analysis of full-length (FL), truncated or antisense (AS) MIR100HG transcripts; Bottom: immunoblots for hnRNPA2B1 pulled-down by the indicated transcripts of MIR100HG. Representative of three independent experiments. e Diagrams of FL and domain-truncated fragments of hnRNPA2B1. RRM, RNA recognition motif; PrLD, prion-like domain. f Detection of MIR100HG by RIP assay as retrieved by Flag-tagged FL or domain-truncated hnNRNPA2B1 using a Flag antibody. An IgG antibody served as a negative control. n = 3 independent biological replicates. g Immunoblots of indicated EMT markers in CC-CR and LoVo cells after hnRNPA2B1 knockdown. Representative of three independent experiments. h Colony counts of 3D-cultured CC-CR cells after hnRNPA2B1 knockdown in the presence or absence of CTX (3 μg/ml), n = 3 independent experiments performed in triplicate. i Extent of migration and invasion using Transwell migration and invasion assays for indicated cells after hnRNPA2B1 knockdown. n = 3 independent biological replicates. j Immunoblots for E-cadherin in CC and SW480 cells with indicated treatment. Representative of three independent experiments. k Colony counts of 3D-cultured MIR100HG^KOE4 CC-CR cells transduced with hnRNPA2B1-expressing lentiviral particles in the presence or absence of CTX (3 μg/ml), n = 3 independent experiments performed in triplicate. l Extent of migration and invasion using Transwell migration and invasion assays for SW480 and DiFi cells with the indicated treatment. n = 3 independent biological replicates. ***P < 0.001, **P < 0.01, *P < 0.05. Data represent mean ± s.d., n.s., not significant