Echinoid is a component of adherens junctions that cooperates with DE-Cadherin to mediate cell adhesion.
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.
Wei
Shu-Yi
SY
Institute of Molecular Medicine, Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan 30034, Republic of China.
Escudero
Luis M
LM
Yu
Fengwei
F
Chang
Li-Hsun
LH
Chen
Li-Ying
LY
Ho
Yu-Huei
YH
Lin
Chiao-Ming
CM
Chou
Chin-Shun
CS
Chia
William
W
Modolell
Juan
J
Hsu
Jui-Chou
JC
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
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