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. 2019 Nov 7;38:457. doi: 10.1186/s13046-019-1449-8

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 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.

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Fig. 5 — CEP disrupts the interaction/colocalization of MYO1C/F-actin with LC3 and LAMP1. MDA-MB-231 cells were treated without or with CEP (4 μM) or Rapa (0.25 μM) for 24 h. a Whole-cell lysate was prepared and subjected to immunoprecipitation using anti-LC3 and the associated MYO1C and actin were determined using immunoblotting. b The fluorescent images of MDA-MB-231 cells immunostained for MYO1C (blue), F-actin (green) and LC3 (red). c LAMP1 was immunoprecipitated, and the expressions of MYO1C and actin were determined by western blot analysis. d The fluorescent images of cells immunostained for MYO1C (blue), F-actin (green) and LAMP1 (red). e The number of LC3 puncta colocalized with MYO1C and F-actin was quantified from 50 cells in three dependent experiments, data was present as mean ± SD (*P < 0.05; **P < 0.01). f The number of LAMP1 puncta colocalized with MYO1C and F-actin was quantified from 50 cells in three dependent experiments, data was present as mean ± SD (*P < 0.05; **P < 0.01)