RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/18824598http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18824598http://www.w3.org/2000/01/rdf-schema#comment"Controlled regulation of Rho GTPase activity is an essential component mediating growth factor-stimulated migration. We have previously shown that angiomotin (Amot), a membrane-associated scaffold protein, plays a critical role during vascular patterning and endothelial migration during embryogenesis. However, the signaling pathways by which Amot controls directional migration are not known. Here we have used peptide pull-down and yeast 2-hybrid (Y2H) screening to identify proteins that interact with the C-terminal PDZ-binding motifs of Amot and its related proteins AmotL1 and 2. We report that Amot and its related proteins bind to the RhoA GTPase exchange factor (RhoGEF) protein Syx. We show that Amot forms a ternary complex together with Patj (or its paralogue Mupp1) and Syx. Using FRET analysis, we provide evidence that Amot controls targeting of RhoA activity to lamellipodia in vitro. We also report that, similar to Amot, morpholino knockdown of Syx in zebrafish results in inhibition of migration of intersegmental arteries. Taken together, our results indicate that the directional migration of capillaries in the embryo is governed by the Amot:Patj/Mupp1:Syx signaling that controls local GTPase activity."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.org/dc/terms/identifier"doi:10.1182/blood-2008-04-153874"xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Liu M."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Majumdar A."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Audebert S."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Schlueter M."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Sinha I."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Aase K."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Ernkvist M."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Holmgren L."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Borg J.P."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Lecine P."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Weide T."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Horowitz A."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/author"Luna Persson N."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/pages"244-253"xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/title"The Amot/Patj/Syx signaling complex spatially controls RhoA GTPase activity in migrating endothelial cells."xsd:string
http://purl.uniprot.org/citations/18824598http://purl.uniprot.org/core/volume"113"xsd:string
http://purl.uniprot.org/citations/18824598http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18824598
http://purl.uniprot.org/citations/18824598http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18824598
http://purl.uniprot.org/uniprot/Q8VHG2#attribution-A3B807249C5FCC633E361AF50D7BFD9Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18824598
http://purl.uniprot.org/uniprot/A0A8M2B9C2#attribution-0F313316C1269F6AFBA4822940D2B467http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18824598