Journal of Biological Chemistry · 2000 · 37 citations · 54 references
Life SciencesCell BiologyDevelopmental BiologyCell AdhesionGene ExpressionMolecular Cell BiologyCell Signaling NetworksDevelopmental Signaling PathwaysCadherin-mediated Cell-cell AdhesionCell-cell Adhesion ComplexesCell-cell Adhesion ForcesMotility MechanismsPoint MutationsWestern Blot AnalysisXenopus Developmental Models
The catenin ARVCF is a member of the p120(ctn) subfamily of Armadillo proteins. A number of catenins directly bind cadherin cytoplasmic tails, contributing to the modulation of cell-cell adhesion and motility processes. Some catenins, such as beta-catenin (and likely p120(ctn)), have additional roles within signaling pathways regulating gene transcription. We have isolated the Xenopus homolog of human ARVCF. Utilizing the cadherin membrane proximal region known to bind p120(ctn) and delta-catenin, coimmunoprecipitation experiments demonstrate that Xarvcf, likewise, binds cadherin in this region and that corresponding point mutations within conserved residues abrogate the Xarvcf-cadherin association. Western blot analysis of Xarvcf protein across a series of developmental stages reveals changes in protein mobility, likely due to changes in phosphorylation. Xarvcf is a maternally provided transcript and expressed in the embryo throughout all stages of development. Interestingly, Xarvcf mRNA is differentially spliced to produce several isoforms, one of which is developmentally regulated. In common with the putative post-translational modifications of the Xarvcf protein, the presence of alternative splice isoforms suggests that Xarvcf possesses the capacity to effect developmental functions in a regulatable manner.
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