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. 2007 May 31;26(12):2942–2954. doi: 10.1038/sj.emboj.7601736

Figure 3.

Figure 3

GST pull-down and immunoprecipitation demonstrate interactions between Oct-25, VegT and Tcf3. (A) Radiolabeled VegT bound to GST/Oct-25 fusion protein and vice versa, but β-Catenin did not interact with GST/Oct-25. Radiolabeled Tcf3 interacted with GST/Oct-25 and vice versa. Radiolabeled β-Catenin was precipitated by GST/Oct-25, when in vitro translated unlabeled Tcf3 was simultaneously added. (B) Both VegT and Tcf3 bound to Oct-60, Oct-91 as well as mouse Oct-3/4. (C) Radiolabeled Tcf3 bound to GST/VegT fusion protein and vice versa. In contrast, VegT did not interact with GST/β-Catenin. (D) VegT did not interact with 1–190 aa, but interacted with 191–397 aa and 398–551 aa regions of Tcf3. Vice versa, Tcf3 interacted with the N-terminal region (1–120 aa) but did not interact with the C-terminal region (121–456 aa) of VegT. (E) Co-immunoprecipitation with anti-myc antibody (IP:α-myc) showed that both myc-tagged Tcf3 (Tcf3-MT) and VegT (VegT-MT) precipitated endogenous Oct-25, whereas anti-flag antibody (IP:α-flag) precipitated a complex of flag-tagged Tcf3 (flag-Tcf3) and VegT-MT and a ternary complex of flag-tagged Oct-25 (flag–Oct-25), Tcf3-MT and VegT-MT.