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Figure 5. Kdm2a Disrupts the Formation of the β-Catenin/Tcf7l1 Complex (A) CoIP detection of the interfering effect of Kdm2a or the mutants on the formation of β-catenin/Tcf7l1 complex. (B and C) The wild-type and mutant β-catenin showed different binding affinity to transfected Tcf7l1 (B) or endogenous TCF7L1 (C). (D) The N-terminal regions of β-catenin showed different binding affinities to endogenous TCF7L1. (E and F) β-catenin with deletions (E) and point mutations (F) showed different activities in the stimulation of luciferase reporter. Error bars represent SEM of four replicates. ∗p < 0.05; ∗∗p < 0.01; ns, not significant. (G) A proposed model for the Kdm2a/Kdm2b-regulated stability of nuclear β-catenin. (See text for details.) In (A)–(D), “Lysate” indicates WCL. Immunoprecipitates were used for all other IB.

Image published in: Lu L et al. (2015)

Copyright © 2015. Image reproduced with permission of the Publisher, Elsevier B. V.

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