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. 2022 Apr 12;12:844477. doi: 10.3389/fonc.2022.844477

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Copyright © 2022 Ning, Sun, Su, Tan, Tang, Sayed, Li, Xue, Liu, Chen and Lu

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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CK1δ/ϵ promotes β-catenin acetylation through enhancing the association of β-catenin with Tip60. (A–C) HEK293T cells were transfected with CK1δ-GFP, CK1ϵ-Flag and CK1α-Flag expression plasmids, and cell lysates were immunoprecipitated with anti-β-catenin agarose beads. The interaction between β-catenin and some histone acetyltransferases (Tip60, PCAF, p300, and CBP) was detected by immunoblotting. (D, E) HEK293T cells were transfected with control vector or Tip60-Flag expression plasmid in the presence or the absence of either CK1δ-Flag (D) or CK1ϵ-Flag (E) expression vector. The β-catenin protein was pulled down with anti-β-catenin agarose beads. The expression of β-catenin, acetylated β-catenin at K49, Flag-tagged proteins and GAPDH was detected by Western blotting. (F–H) HEK293T cells were transfected with control vector or Tip60-Flag expression plasmid in the presence or absence of either CK1δ-GFP (F) or CK1ϵ-V5 (G) or CK1α-V5 (H) expression plasmids. Whole cell lysates were immunoprecipitated with anti-Flag agarose beads. The expression of serine-phosphorylated Tip60, Tip60-Flag, CK1δ-GFP, CK1ϵ-V5, CK1α-V5 and GAPDH was measured by Western blotting. The expression of serine-phosphorylated Tip60 was detected by an anti-phospho-serine antibody.