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. 1999 Jun;19(6):4503–4515. doi: 10.1128/mcb.19.6.4503

FIG. 4.

FIG. 4

β-Catenin does not interact with importin α2 or importin β. A GST pull-down experiment with 35S-labeled, in vitro-translated wild-type β-catenin, importin α2, and recombinant GST-importin β was performed. An N-terminal deletion mutant of importin α2 that removes the importin β interaction domain (ΔN importin α2) was included as a negative control for nonspecific binding. The first three lanes indicate the amount of importin α2 and β-catenin proteins added (10% input). While full-length (FL) importin α2 readily interacts with GST-importin β, β-catenin does not, either in the presence or absence of importin α2.