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. 2022 Nov 7;8:449. doi: 10.1038/s41420-022-01234-8

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© The Author(s) 2022

Open Access This 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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 6 — A After immunoblot analysis,the gel were stained with coomassie brilliant blue and the bands that were precipitated specifically by SHIP2 underwent mass spectrometric detection. B The binding of LINC01468 to CUL4A was revealed by LINC01468 pull-down followed by immunoblot analysis. C RIP assay showed that LINC01468 binds to CUL4A. The data represent the means ± S.D (**P < 0.01). D Co-IP showed the binding of SHIP2 to CUL4A. E Huh7 cells transfected with siCUL4A or F SNU-449 cells transfected with CUL4A-Flag plasmid were submitted to examine SHIP2 and CUL4A by western blotting. G CUL4A promotes SHIP2 ubiquitination. SNU-449 cells transfected with or without CUL4A-Flag plasmid were treated with MG132 (5 μM for 4 h), after which cells were subjected to Co-IP with SHIP2. H LINC01468 silencing decreased the interaction of SHIP2 with CUL4A. I Knockdown of CUL4A abrogated the LINC01468-mediated degradation of SHIP2 protein. J Silencing of CUL4A prolonged the degradation of SHIP2. Immunoblotting detection of His tag is shown. K Knockdown of LINC01468 reduced the ubiquitination of SHIP2. L Knockdown of CUL4A reduced the ubiquitination of SHIP2. The input of the cell lysates were showed in the bottom panels.