Regulation of E-cadherin/catenin association by tyrosine phosphorylation.

Abstract

VOLUME 274 (1999) PAGES 36734–36740 Several concerns were raised about Figs. 3, 4, and 5 by the journal. Because the original data were no longer available, the experiments shown in these figures were repeated. The repeated experiments are shown and do not affect the results or conclusions of this work. The authors regret the inconvenience these errors may have produced.View Large Image Figure ViewerDownload Hi-res image Download (PPT)FIGURE 5Binding of β-catenin point mutants to the cytosolic domain of E-cadherin. Panel A, 0.32 pmol (30 ng) of wild-type β-catenin (WT), Tyr-86 → Phe mutant (Y86F) or Tyr-654 → Phe mutant (Y654F) were phosphorylated by pp60c-src and incubated with 1.2 pmol of either cytoEcad-GST or GST, in a final volume of 200 μl as described under “Experimental Procedures.” Analysis of β-catenin bound was performed as previously indicated. The numbers below the lanes indicate the amount of β-catenin bound normalized to non-phosphorylated β-catenin WT. Panel C, a binding assay similar to that described in panel A was also performed with equivalent amounts of Tyr-86 → Glu (Y86E) or Tyr-654 → Glu (Y654E) mutants. The numbers below the lanes indicate the amount of β-catenin bound that were calculated comparing the result of the scanning of the corresponding lanes with a known amount of β-catenin included as reference in the same blot (St). No signal was detected when GST was used as bait. Although not shown, the anti-β-catenin mAb used in our assays reacted identically with all of the β-catenin forms analyzed.View Large Image Figure ViewerDownload Hi-res image Download (PPT)