| http://purl.uniprot.org/citations/15817639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15817639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15817639 | http://www.w3.org/2000/01/rdf-schema#comment | "We have previously identified C1 domain-containing phosphatase and TENsin homologue (C1-TEN) as being an intracellular binding partner for Axl receptor tyrosine kinase (RTK). C1-TEN is a tensin-related protein that houses an N-terminal region with predicted structural similarity to PTEN. Here, we report our observations on the effects of ectopic expression of C1-TEN in HEK293 cells, which resulted in profound molecular and phenotypic changes. Stable expression of C1-TEN altered cellular morphology, with less cell spreading and weaker filamentous actin staining. Cells overexpressing C1-TEN were inhibited greatly in their proliferation and migration rates as compared with mock-transfected cells. Furthermore, serum starvation-induced apoptosis caused a twofold increase in caspase 3 activity in C1-TEN-overexpressing cells vs. mock cells. In addition, C1-TEN-overexpressing cells showed a markedly reduced phosphorylation of Akt/PKB kinase and its substrate GSK3, as well as reduced Akt enzymatic activity. No such effects on JNK were observed. Also, serum-stimulated activation of Akt was delayed in C1-TEN-overexpressing cells, while no difference in profile of ERK activation was observed. Furthermore, cells expressing a C1-TEN mutant where the putative phosphatase active site cysteine at position 231 was substituted for a serine displayed full restoration of both cell proliferation and Akt activation. In conclusion, C1-TEN appears to be a novel intracellular phosphatase that negatively regulates the Akt/PKB signaling cascade, and is similar to its relative PTEN in this respect. However, the particular domain organization of C1-TEN may enable it to regulate RTK and other signaling complexes that are linked to Akt/PKB signaling in a unique manner."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.org/dc/terms/identifier | "doi:10.1096/fj.04-2532fje"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.org/dc/terms/identifier | "doi:10.1096/fj.04-2532fje"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Dahlbaeck B."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Dahlbaeck B."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Hafizi S."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Hafizi S."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Ibraimi F."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/author | "Ibraimi F."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/name | "FASEB J."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/name | "FASEB J."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/pages | "971-973"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/pages | "971-973"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/title | "C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway and inhibits cell survival, proliferation, and migration."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/title | "C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway and inhibits cell survival, proliferation, and migration."xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/15817639 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15817639 |
| http://purl.uniprot.org/citations/15817639 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15817639 |
| http://purl.uniprot.org/citations/15817639 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15817639 |
| http://purl.uniprot.org/citations/15817639 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15817639 |