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Dev Cell. 2005 Apr;8(4):493-504.

Echinoid is a component of adherens junctions that cooperates with DE-Cadherin to mediate cell adhesion.

Author information

1
Institute of Molecular Medicine, Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan 30034, Republic of China.

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.

PMID:
15809032
DOI:
10.1016/j.devcel.2005.03.015
[Indexed for MEDLINE]
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