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. 2020 Mar 18;19:60. doi: 10.1186/s12943-020-01184-8

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© The Author(s) 2020

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. 5 — circLONP2 directly interacts with DDX1. a Different protein bands detected by silver stain for mass spectrometry. b KEGG analysis of potential proteins interacting with circLONP2. c The specific amino acid sequence of DDX1 showed by second-order mass spectrum. d RNA pulldown followed by WB confirmed the interaction of circLONP2 with DDX1, DDX5 and DDX17. e, f A series of deletion mutants of DDX1 labeled with FLAG and confirmed by WB. g Anti-FLAG RIP assay showed significant enrichment of circLONP2 in SPRY domain and the full length of DDX1. h, i Rescue experiments indicated that DDX1 was essential for circLONP2-enhanced migrating ability of CRC cells. All experiments were repeated for three times, data were shown as mean ± SD, * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 in one-way ANOVA (g-i)