Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.devcel.2005.03.015
Title: Echinoid is a component of adherens junctions that cooperates with DE-cadherin to mediate cell adhesion
Authors: Wei, S.-Y.
Escudero, L.M.
Yu, F. 
Chang, L.H.
Chen, L.-Y.
Ho, Y.-H.
Lin, C.-M.
Chou, C.-S.
Chia, W. 
Modolell, J.
Hsu, J.-C.
Issue Date: Apr-2005
Citation: Wei, S.-Y., Escudero, L.M., Yu, F., Chang, L.H., Chen, L.-Y., Ho, Y.-H., Lin, C.-M., Chou, C.-S., Chia, W., Modolell, J., Hsu, J.-C. (2005-04). Echinoid is a component of adherens junctions that cooperates with DE-cadherin to mediate cell adhesion. Developmental Cell 8 (4) : 493-504. ScholarBank@NUS Repository. https://doi.org/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 β-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. Copyright © 2005 by Elsevier Inc.
Source Title: Developmental Cell
URI: http://scholarbank.nus.edu.sg/handle/10635/113449
ISSN: 15345807
DOI: 10.1016/j.devcel.2005.03.015
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