1. Binding site for p120/delta-catenin is not required for Drosophila E-cadherin function in vivo
- Author
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Li Lin, Anne Pacquelet, and Pernille Rørth
- Subjects
Male ,Delta Catenin ,animal structures ,Embryo, Nonmammalian ,CHO Cells ,Biology ,Congenital Abnormalities ,Cell membrane ,Oogenesis ,Cell Movement ,Cricetinae ,Report ,medicine ,Cell Adhesion ,Animals ,Cell adhesion ,Body Patterning ,Cell Aggregation ,Armadillo Domain Proteins ,Binding Sites ,Cell adhesion molecule ,Cadherin ,Cell Membrane ,cell adhesion ,oogenesis ,migration ,morphogenesis ,adherens junction ,Gene Expression Regulation, Developmental ,Catenins ,Cell Biology ,Cell sorting ,Actin cytoskeleton ,Cadherins ,Phosphoproteins ,Cell aggregation ,Cell biology ,Protein Structure, Tertiary ,Cytoskeletal Proteins ,medicine.anatomical_structure ,Drosophila melanogaster ,Catenin ,Models, Animal ,Mutation ,Female ,Cell Adhesion Molecules - Abstract
Homophilic cell adhesion mediated by classical cadherins is important for many developmental processes. Proteins that interact with the cytoplasmic domain of cadherin, in particular the catenins, are thought to regulate the strength and possibly the dynamics of adhesion. beta-catenin links cadherin to the actin cytoskeleton via alpha-catenin. The role of p120/delta-catenin proteins in regulating cadherin function is less clear. Both beta-catenin and p120/delta-catenin are conserved in Drosophila. Here, we address the importance of cadherin-catenin interactions in vivo, using mutant variants of Drosophila epithelial cadherin (DE-cadherin) that are selectively defective in p120ctn (DE-cadherin-AAA) or beta-catenin-armadillo (DE-cadherin-Delta beta) interactions. We have analyzed the ability of these proteins to substitute for endogenous DE-cadherin activity in multiple cadherin-dependent processes during Drosophila development and oogenesis; epithelial integrity, follicle cell sorting, oocyte positioning, as well as the dynamic adhesion required for border cell migration. As expected, DE-cadherin-Delta beta did not substitute for DE-cadherin in these processes, although it retained some residual activity. Surprisingly, DE-cadherin-AAA was able to substitute for the wild-type protein in all contexts with no detectable perturbations. Thus, interaction with p120/delta-catenin does not appear to be required for DE-cadherin function in vivo.
- Published
- 2003