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. 2025 Aug 12;16:1630311. doi: 10.3389/fimmu.2025.1630311

Figure 4.

Experimental data on the interaction between KCTD10 and β-catenin. Panels A, D, and C show co-immunoprecipitation results demonstrating binding. Panel B illustrates domain structures. Panel E indicates β-catenin protein stability in the presence of KCTD10 over time. Panels F and H show protein levels under various conditions. Panel G features fluorescence microscopy images of cells stained for DAPI, KCTD10, and β-catenin. Panels I, J, and K present ubiquitination assays with different Lysine mutations, indicating how KCTD10 affects β-catenin ubiquitination.

KCTD10 promotes ubiquitination and degradation of β-catenin through the K48-ubiquitin chain. (A) Co-IP analysis demonstrating the interaction between KCTD10 and β-catenin proteins. (B) Representative schematic of KCTD10 and β-catenin protein domains. (C, D) Identification of the interacting regions between truncated KCTD10 and β-catenin proteins. (E) Degradation of β-catenin proteins after CHX treatment. (F) Effect of KCTD10 on β-catenin protein stability in the presence of MG132. (G, H) Fluorescence analysis and Western blots showing KCTD10-induced degradation of cytoplasmic β-catenin. (I–K) KCTD10 overexpression enhanced the ubiquitination of β-catenin. Myc-β-catenin was immunoprecipitated with rabbit polyclonal anti-β-catenin antibodies and these immunocomplexes were subjected to Western blotting with anti-ubiquitin antibodies to detect β-catenin-ubiquitin conjugates. In the ubiquitin constructs, R indicates that the corresponding lysine residue has been mutated to arginine, abolishing linkage at that site; O indicates that only the corresponding lysine residue remains intact, while all other lysines are mutated, allowing selective assessment of linkage through that specific site.