| http://purl.uniprot.org/citations/18833327 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18833327 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundThe epidermal cells of the C. elegans embryo undergo coordinated cell shape changes that result in the morphogenetic process of elongation. The cytoskeletal ankyrin repeat protein VAB-19 is required for cell shape changes and localizes to cell-matrix attachment structures. The molecular functions of VAB-19 in this process are obscure, as no previous interactors for VAB-19 have been described.Methodology/principal findingsIn screens for VAB-19 binding proteins we identified the signaling adaptor EPS-8. Within C. elegans epidermal cells, EPS-8 and VAB-19 colocalize at cell-matrix attachment structures. The central domain of EPS-8 is necessary and sufficient for its interaction with VAB-19. eps-8 null mutants, like vab-19 mutants, are defective in epidermal elongation and in epidermal-muscle attachment. The eps-8 locus encodes two isoforms, EPS-8A and EPS-8B, that appear to act redundantly in epidermal elongation. The function of EPS-8 in epidermal development involves its N-terminal PTB and central domains, and is independent of its C-terminal SH3 and actin-binding domains. VAB-19 appears to act earlier in the biogenesis of attachment structures and may recruit EPS-8 to these structures.Conclusions/significanceEPS-8 and VAB-19 define a novel pathway acting at cell-matrix attachments to regulate epithelial cell shape. This is the first report of a role for EPS-8 proteins in cell-matrix attachments. The existence of EPS-8B-like isoforms in Drosophila suggests this function of EPS-8 proteins could be conserved among other organisms."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0003346"xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "Ding M."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "Chisholm A.D."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "Hardin J."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "King R.S."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/author | "Berry E.C."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/name | "PLoS One"xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/pages | "e3346"xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/title | "The cell signaling adaptor protein EPS-8 is essential for C. elegans epidermal elongation and interacts with the ankyrin repeat protein VAB-19."xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://purl.uniprot.org/core/volume | "3"xsd:string |
| http://purl.uniprot.org/citations/18833327 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18833327 |
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