title: Echinoid is a component of adherens junctions that cooperates with DE-Cadherin to mediate cell adhesion.
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.
authors.affiliation: Institute of Molecular Medicine, Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan 30034, Republic of China.
authors.forename: Shu-Yi
authors.initials: SY
authors.lastname: Wei
authors.forename: Luis M
authors.initials: LM
authors.lastname: Escudero
authors.forename: Fengwei
authors.initials: F
authors.lastname: Yu
authors.forename: Li-Hsun
authors.initials: LH
authors.lastname: Chang
authors.forename: Li-Ying
authors.initials: LY
authors.lastname: Chen
authors.forename: Yu-Huei
authors.initials: YH
authors.lastname: Ho
authors.forename: Chiao-Ming
authors.initials: CM
authors.lastname: Lin
authors.forename: Chin-Shun
authors.initials: CS
authors.lastname: Chou
authors.forename: William
authors.initials: W
authors.lastname: Chia
authors.forename: Juan
authors.initials: J
authors.lastname: Modolell
authors.forename: Jui-Chou
authors.initials: JC
authors.lastname: Hsu
mesh_terms: D000199:Actins / Q000378:metabolism; D022005:Adherens Junctions / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D015820:Cadherins / Q000235:genetics / Q000378:metabolism*; D002448:Cell Adhesion / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism*; D048430:Cell Shape; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000033:anatomy & histology / Q000235:genetics / Q000254:growth & development / Q000378:metabolism; D004628:Embryonic Structures / Q000166:cytology / Q000378:metabolism; D047908:Intracellular Signaling Peptides and Proteins / Q000235:genetics / Q000378:metabolism; D009024:Morphogenesis; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D014921:Wings, Animal / Q000166:cytology / Q000254:growth & development
chemical_list: D000199:Actins; D015820:Cadherins; D015815:Cell Adhesion Molecules; D029721:Drosophila Proteins; C422623:ED protein, Drosophila; D047908:Intracellular Signaling Peptides and Proteins; D011993:Recombinant Fusion Proteins; D012097:Repressor Proteins; C400774:baz protein, Drosophila; C501889:shg protein, Drosophila