| http://purl.uniprot.org/citations/15148318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15148318 | http://www.w3.org/2000/01/rdf-schema#comment | "Endoglin is a component of the transforming growth factor-beta receptor complex abundantly expressed at the surface of endothelial cells and plays an important role in cardiovascular development and vascular remodeling. By using the cytoplasmic domain of endoglin as a bait for screening protein interactors, we have identified ZRP-1 (zyxin-related protein 1), a 476-amino acid member that belongs to a family of LIM containing proteins that includes zyxin and lipoma-preferred partner. The endoglin interacting region was mapped within the three double zinc finger LIM domains of the ZRP-1 C terminus. Analysis of the subcellular distribution of ZRP-1 demonstrated that in the absence of endoglin, ZRP-1 mainly localizes to focal adhesion sites, whereas in the presence of endoglin ZRP-1 is found along actin stress fibers. Because the LIM family of proteins has been shown to associate with the actin cytoskeleton, we investigated the possibility of a regulatory role for endoglin with regard to this structure. Expression of endoglin resulted in a dramatic reorganization of the actin cytoskeleton. In the absence of endoglin, F-actin was localized to dense aggregates of bundles, whereas in the presence of endoglin, expressed in endothelial cells, F-actin was in stress fibers and colocalized with ZRP-1. Furthermore, small interfering RNA-mediated suppression of endoglin or ZRP-1, or clustering of endoglin in endothelial cells, led to mislocalization of F-actin fibers. These results suggest a regulatory role for endoglin, via its interaction with ZRP-1, in the actin cytoskeletal organization."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m400843200"xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Banville D."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Bernabeu C."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Botella L.M."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Vary C.P."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Guerrero-Esteo M."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/author | "Sanz-Rodriguez F."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/pages | "32858-32868"xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/title | "Endoglin regulates cytoskeletal organization through binding to ZRP-1, a member of the Lim family of proteins."xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://purl.uniprot.org/core/volume | "279"xsd:string |
| http://purl.uniprot.org/citations/15148318 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15148318 |
| http://purl.uniprot.org/citations/15148318 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15148318 |
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| http://purl.uniprot.org/uniprot/#_F2ZC06-mappedCitation-15148318 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15148318 |
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