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. 2021 Jun 7;40:187. doi: 10.1186/s13046-021-01977-9

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© The Author(s) 2021

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. 6 — ARST interacted with the binding sites of ALDOA and F-actin. A, B The catRAPID database was referenced to predict the binding domains of ARST and ALDOA. C Truncated ARST was demonstrated by the diagrammatic sketch. The binding domain predicted by catRAPID was highlighted in yellow. D RNA pulldown followed by western blot was performed to detect the binding capacity of truncated ALDOA with ARST. E The mutation sites on ARST, highlighted by red arrows, were demonstrated by diagrammatic sketch. F RNA pulldown followed by western blot was performed to detect the interactive capacities of different mutant ALDOA with ARST. G Co-immunoprecipitation assay was performed to detect the binding capacity of F-actin and cofilin in the presence of ALDOA mutants. All results were presented as mean ± s.d. from three independent experiments (****P < 0.001)