| http://purl.uniprot.org/citations/14709717 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14709717 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/14709717 | http://www.w3.org/2000/01/rdf-schema#comment | "The receptor protein tyrosine phosphatase density-enhanced phosphatase-1 (DEP-1) has been implicated in aberrant cancer cell growth and immune cell function, however, its function within cells has yet to be properly elucidated. To investigate the cellular function of DEP-1, stable cell lines inducibly expressing DEP-1 were generated. Induction of DEP-1 expression was found to decrease PDGF-stimulated tyrosine phosphorylation of a number of cellular proteins including the PDGF receptor, and to inhibit growth factor-stimulated phosphorylation of components of the MAPK pathway, indicating that DEP-1 antagonised PDGF receptor signalling. This was supported by data showing that DEP-1 expression resulted in a reduction in cell proliferation. DEP-1-expressing cells had fewer actin-containing microfilament bundles, reduced vinculin and paxillin-containing adhesion plaques, and were defective in interactions with fibronectin. Defective cell-substratum adhesion correlated with lack of activation of FAK in DEP-1-expressing cells. Time-lapse interference reflection microscopy of live cells revealed that although small focal contacts at the leading edge were generated in DEP-1-expressing cells, they failed to mature into stable focal adhesions, as found in control cells. Further motility analysis revealed that DEP-1-expressing cells retained limited random motility, but showed no chemotaxis towards a gradient of PDGF. In addition, cell-cell contacts were disrupted, with a change in the localisation of cadherin from discrete areas of cell-cell contact to large areas of membrane interaction, and there was a parallel redistribution of beta-catenin. These results demonstrate that DEP-1 is a negative regulator of cell proliferation, cell-substratum contacts, motility and chemotaxis in fibroblasts."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.00879"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.00879"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Kellie S."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Kellie S."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Bird I.N."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Bird I.N."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Jones G.E."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Jones G.E."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Craggs G."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/author | "Craggs G."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/pages | "609-618"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/pages | "609-618"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/title | "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/title | "The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation."xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/volume | "117"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://purl.uniprot.org/core/volume | "117"xsd:string |
| http://purl.uniprot.org/citations/14709717 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14709717 |
| http://purl.uniprot.org/citations/14709717 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/14709717 |