Fig. 6

FOXG1 binds directly to β-catenin. a Immunoprecipitation (IP) assay detected the binding of endogenous FOXG1 and β-catenin. b IP assay detected the binding of exogenous FOXG1 and β-catenin using anti-FOXG1 to pull down, and followed by immunoblotting (IB) with anti-FLAGantibody. c IP assay detected the binding of exogenous FOXG1 and β-catenin using anti-FLAG-β-catenin to pull down and followed by immunoblotting (IB) with anti-FOXG1. d Schematic representation of FLAG-tagged full-size and mutant β-catenin. NH2- (gray) and COOH-terminal (black) domains and the 12 internal armadillo-like repeats of β-catenin are indicated. Six different stretches of unrepeated amino acid deletions of β-catenin and the full-size β-catenin are shown in rows 1–7. Twelve internal armadillo-like repeats are shown as numbered boxes. The positions of the amino acid sequences shown and FOXG1 binding ability appear at right. e Protein lysates were immunoprecipitated with FLAG anti serum. Equivalent fractions of the immunoprecipitates were separated by SDS-PAGE and blotted with the indicated monoclonal antibodies to analyze binding of mutant β-catenin to FOXG1