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Fig. 4. Wg signaling leads to an increase of cadherin-independent pools of Arm and -catenin. NP-40 lysates of heat shocked cl8mEcad cells (A), cl8Dshmyc cells induced by Cu²⁺ (B) and heat shocked cl8HSDsh/mEcad cells (C) were fractionated under nondenaturing conditions by FPLC gel filtration. (A) In extracts of cl8mEcad cells, Arm was detected only in fractions containing E-cadherin, and more than 90% of -catenin was also present in these fractions. (B) In cl8Dshmyc cells induced to overexpress Dsh, Arm was present exclusively in low molecular mass fractions together with the majority of -catenin. (C) Overexpression of Dsh in cl8HSDsh/mEcad cells led to the appearance of Arm and -catenin in low molecular mass fractions devoid of E-cadherin. The distribution of E-cadherin itself remained unaltered. Note that -catenin showed an altered distribution despite the fact that the total amount is unaffected by Wg signaling (cf. Fig. 7). Compared with Fig. 3, little phosphorylated Arm was detected in this experiment, presumably because of dephosphorylation during gel filtration chromatography, which was performed under non-denaturing conditions. Fractionation peaks of molecular mass markers are indicated at the bottom. The exposure times of ECL-treated western blots were optimized for each fractionation experiment and thus do not allow any quantitative comparison of protein levels between different panels.

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