http://purl.uniprot.org/citations/15809032 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15809032 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.devcel.2005.03.015"xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Yu F."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Modolell J."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Chia W."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Ho Y.H."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Hsu J.C."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Lin C.M."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Chang L.H."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Chen L.Y."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Escudero L.M."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Wei S.Y."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/author | "Chou C.S."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/name | "Dev Cell"xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/pages | "493-504"xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/title | "Echinoid is a component of adherens junctions that cooperates with DE-Cadherin to mediate cell adhesion."xsd:string |
http://purl.uniprot.org/citations/15809032 | http://purl.uniprot.org/core/volume | "8"xsd:string |
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http://purl.uniprot.org/citations/15809032 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15809032 |
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http://purl.uniprot.org/uniprot/M9PCI6#attribution-1E7C630C4D8FEF94752D96540B611076 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15809032 |
http://purl.uniprot.org/uniprot/M9PCI6#attribution-DA3B5C34A2B8BF95B42C900FB64EFF5F | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15809032 |