| http://purl.uniprot.org/citations/17540773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17540773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17540773 | http://www.w3.org/2000/01/rdf-schema#comment | "In endothelial cells, transforming growth factor beta (TGF-beta) signals through two distinct pathways to regulate endothelial cell proliferation and migration, the ALK-1/Smads 1/5/8 pathway and the ALK-5/Smads 2/3 pathway. TGF-beta signaling through these pathways is further regulated in endothelial cells by the endothelial specific TGF-beta superfamily co-receptor, endoglin. The importance of endoglin, ALK-1, and ALK-5 in endothelial biology is underscored by the embryonic lethal phenotypes of knock-outs in mice due to defects in angiogenesis, and by the presence of disease-causing mutations in these genes in human vascular diseases. However, the mechanism of action of endoglin is not well defined. Here we define a novel interaction between endoglin and the scaffolding protein beta-arrestin2. Both co-immunoprecipitation and fluorescence confocal studies demonstrate the specific interaction between endoglin and beta-arrestin2 in endothelial cells, enhanced by ALK-1 and to a lesser extent by the type II TGF-beta receptor. The endoglin/beta-arrestin2 interaction results in endoglin internalization and co-accumulation of endoglin and beta-arrestin2 in endocytic vesicles. Whereas endoglin did not have a direct impact on either Smad 2/3 or Smad 1/5/8 activation, endoglin antagonized TGF-beta-mediated ERK signaling, altered the subcellular distribution of activated ERK, and inhibited endothelial cell migration in a manner dependent on the ability of endoglin to interact with beta-arrestin2. Reciprocally, small interfering RNA-mediated silencing of endogenous beta-arrestin2 expression restored TGF-beta-mediated ERK activation and increased endothelial cell migration in an endoglin-dependent manner. These studies define a novel function for endoglin, and further expand the roles mediated by the ubiquitous scaffolding protein beta-arrestin2."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m700176200"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m700176200"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/author | "Blobe G.C."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/author | "Blobe G.C."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/author | "Lee N.Y."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/author | "Lee N.Y."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/pages | "21507-21517"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/pages | "21507-21517"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/title | "The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/title | "The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells."xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://purl.uniprot.org/core/volume | "282"xsd:string |
| http://purl.uniprot.org/citations/17540773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17540773 |
| http://purl.uniprot.org/citations/17540773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17540773 |
| http://purl.uniprot.org/citations/17540773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17540773 |
| http://purl.uniprot.org/citations/17540773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17540773 |
| http://purl.uniprot.org/uniprot/P17813 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17540773 |
| http://purl.uniprot.org/uniprot/Q91YI4 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17540773 |