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. 2022 May 23;11(1):28. doi: 10.1038/s41389-022-00402-w

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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. 1 — A The collection of palmitoylated proteins and cancer driver genes in GBM. B The interaction of HA-ZDHHC4 with GFP-GSK3α and GFP-GSK3β was verified by immunoprecipitation in 293 T cells. C The localization of ZDHHC4 and GSK3β in SF126 cells was detected by immunofluorescence staining. D Protein map showing the three post-translationally modified amino acid residues in GSK3β. E SF126 cells were transfected, and the experiment was divided into three groups: wild-type Flag-GSK3β, C14A mutant GSK3β, and wild-type Flag-GSK3β were simultaneously knocked down ZDHHC4 by siRNA. ABE analysis and phosphorylation of GSK3α and GSK3β were performed in the three groups. The experiment was repeated twice. F ZDHHC4 was knocked down by siRNA in SF126 cells with stable expression of Flag-GSK3β. Immunoprecipitation assays showed the interaction of Flag-GSK3β with AKT, p70S6K, PKA, and p90RSK.