Echinoid Is a Component of Adherens Junctions That Cooperates With DE-Cadherin to Mediate Cell Adhesion

Dev Cell. 2005 Apr;8(4):493-504. doi: 10.1016/j.devcel.2005.03.015.

Abstract

Echinoid is an immunoglobulin domain-containing transmembrane protein that modulates cell-cell signaling by Notch and the EGF receptors. We show that, in the Drosophila wing disc epithelium, Echinoid is a component of adherens junctions that cooperates with DE-Cadherin in cell adhesion. Echinoid and beta-catenin (a DE-Cadherin interacting protein) each possess a C-terminal PDZ domain binding motif that binds to Bazooka/PAR-3; these motifs redundantly position Bazooka to adherens junctions. Echinoid also links to actin filaments by binding to Canoe/AF-6/afadin. Moreover, interfaces between Echinoid- and Echinoid+ cells, like those between DE-Cadherin- and DE-Cadherin+ cells, are deficient in adherens junctions and form actin cables. These characteristics probably facilitate the strong sorting behavior of cells that lack either of these cell-adhesion molecules. Finally, cells lacking either Echinoid or DE-Cadherin accumulate a high density of the reciprocal protein, further suggesting that Echinoid and DE-Cadherin play similar and complementary roles in cell adhesion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Adherens Junctions / chemistry
  • Adherens Junctions / metabolism*
  • Animals
  • Cadherins / genetics
  • Cadherins / metabolism*
  • Cell Adhesion / physiology*
  • Cell Adhesion Molecules / genetics
  • Cell Adhesion Molecules / metabolism*
  • Cell Shape
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / anatomy & histology
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / growth & development
  • Drosophila melanogaster / metabolism
  • Embryonic Structures / cytology
  • Embryonic Structures / metabolism
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Morphogenesis
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Wings, Animal / cytology
  • Wings, Animal / growth & development

Substances

  • Actins
  • Cadherins
  • Cell Adhesion Molecules
  • Drosophila Proteins
  • ED protein, Drosophila
  • Intracellular Signaling Peptides and Proteins
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • baz protein, Drosophila
  • shg protein, Drosophila