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. 2010 Jan 11;285(11):8472–8480. doi: 10.1074/jbc.M109.069450

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FIGURE 2. — A, immunoprecipitation (IP) of HA-Peg3/Pw1 (upper panels) or endogenous β-catenin (lower panels), followed by Western blotting using anti-HA or anti-β-catenin antibodies. Control (Cont) cells were transfected with empty vector. Both input and immunoprecipitated lysates are shown. Note that HA-Peg3/Pw1 (but not HA-Zim2) co-precipitated with β-catenin. B, schematic diagram of HA-tagged expression constructs for full-length Peg3/Pw1, the N-terminal SCAN domain of Peg3/Pw1 (HA-Peg3SCAN), and the C-terminal zinc finger domains of Peg3/Pw1 (HA-Peg3ZF). C, left panel, anti-HA Western blot (WB) for HA-Peg3/Pw1 (second lane), HA-Peg3SCAN (third lane), and HA-Peg3ZF (fourth lane) illustrating the locations of the respective bands on the gel; right panel, anti-HA Western blot of β-catenin immunoprecipitates after overexpression of HA-Peg3/Pw1 (second lane), HA-Peg3SCAN (third lane), and HA-Peg3ZF (fourth lane). Only HA-Peg3/Pw1 and HA-Peg3SCAN immunoprecipitated with β-catenin. D, Western blot analysis illustrating the effect of HA-Peg3/Pw1, HA-Peg3ZF, HA-Peg3SCAN, Peg3/Pw1 (PlentiPeg3), and control vectors (pCMV and PlentiEGFP) on β-catenin expression in HeLa cells. E, fluorescence micrographs showing immunolocalization of HA-Peg3/Pw1, HA-Peg3ZF, and HA-Peg3SCAN (green) in human 293T cells. Nuclei were counterstained with fluorescein isothiocyanate/4′,6-diamidino-2-phenylindole (FITC/DAPI; blue). Scale bar = ∼4 μm.