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. 2012 Jul 5;4(9):992–1007. doi: 10.1002/emmm.201101043

Figure 1. KLF15 interacts with β-catenin, NLK and TCF4.

Figure 1

The transfected constructs in A, B and C were detected in the protein lysates. IgG isotype (IP-CT) (lane 1) and empty vector (EV) (lane 2) were used as controls; GAPDH served as loading control. (A, B and C) Endogenous validation of the identified interactions between KLF15 and β-catenin, NLK as well as TCF4 in adult cardiac tissue are depicted (lane 8). Lane 9 shows the IgG isotype control for IP. Endogenous detection of KLF15, β-catenin, NLK as well as TCF4 in the different lysates is shown. (*) IgG heavy chain (50 kDa).

  1. Co-immunoprecipitation (IP) analysis showing interaction of KLF15 and β-catenin in HEK293 cells overexpressing cmyc-β-catenin and Flag-KLF15-full-length (lane 3). Co-transfection of truncated (ΔN45, ΔN152, ΔN260)-KLF15 (lane 4–6) or a ΔC-KLF15 (lane 7) and cmyc-β-catenin plasmids in HEK293 cells showing the requirement of the first 45 amino acids of KLF15 for binding β-catenin.
  2. Interaction of NLK with KLF15-full-length, -ΔN45 (lane 3 and 4) and -ΔC (lane 7) were shown by co-IP assays in HEK293.
  3. TCF4 interacted with KLF15-full-length and all N-terminal mutants (lane 3–6), but not with the -ΔC construct (lane 7) in HEK293.