http://purl.uniprot.org/citations/16291724 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16291724 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16291724 | http://www.w3.org/2000/01/rdf-schema#comment | "The carcinoembryonic antigen-related cell adhesion molecule CEACAM1 (CD66a) and the scaffolding protein filamin A have both been implicated in tumor cell migration. In the present study we identified filamin A as a novel binding partner for the CEACAM1-L cytoplasmic domain in a yeast two-hybrid screen. Direct binding was shown by surface plasmon resonance analysis and by affinity precipitation assays. The association was shown for human and rodent CEACAM1-L in endogenous CEACAM1-L expressing cells. To address functional aspects of the interaction, we used a well-established melanoma cell system. We found in different migration studies that the interaction of CEACAM1-L and filamin A drastically reduced migration and cell scattering, whereas each of these proteins when expressed alone, acted promigratory. CEACAM1-L binding to filamin A reduced the interaction of the latter with RalA, a member of the Ras-family of GTPases. Furthermore, co-expression of CEACAM1-L and filamin A led to a reduced focal adhesion turnover. Independent of the presence of filamin A, the expression of CEACAM1-L led to an increased phosphorylation of focal adhesions and to altered cytoskeletal rearrangements during monolayer wound healing assays. Together, our data demonstrate a novel mechanism for how CEACAM1-L regulates cell migration via its interaction with filamin A."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/name | "J. Cell Sci."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02660"xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02660"xsd:string |
http://purl.uniprot.org/citations/16291724 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16291724 |
http://purl.uniprot.org/citations/16291724 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16291724 |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Mueller M.M."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Mueller M.M."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Kannicht C."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Kannicht C."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Klaile E."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Klaile E."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Lucka L."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Lucka L."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Singer B.B."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/author | "Singer B.B."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/pages | "5513-5524"xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/pages | "5513-5524"xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/title | "CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration."xsd:string |
http://purl.uniprot.org/citations/16291724 | http://purl.uniprot.org/core/title | "CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration."xsd:string |