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http://purl.uniprot.org/citations/23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23000962http://www.w3.org/2000/01/rdf-schema#comment"Angiogenesis, the formation of new blood vessels, is fundamental to development and post-injury tissue repair. Vascular endothelial growth factor (VEGF)-A guides and enhances endothelial cell migration to initiate angiogenesis. Profilin-1 (Pfn-1) is an actin-binding protein that enhances actin filament formation and cell migration, but stimulus-dependent regulation of Pfn-1 has not been observed. Here, we show that VEGF-A-inducible phosphorylation of Pfn-1 at Tyr 129 is critical for endothelial cell migration and angiogenesis. Chemotactic activation of VEGF receptor kinase-2 (VEGFR2) and Src induces Pfn-1 phosphorylation in the cell leading edge, promoting Pfn-1 binding to actin and actin polymerization. Conditional endothelial knock-in of phosphorylation-deficient Pfn1(Y129F) in mice reveals that Pfn-1 phosphorylation is critical for angiogenesis in response to wounding and ischaemic injury, but not for developmental angiogenesis. Thus, VEGFR2/Src-mediated phosphorylation of Pfn-1 bypasses canonical, multistep intracellular signalling events to initiate endothelial cell migration and angiogenesis, and might serve as a selective therapeutic target for anti-angiogenic therapy."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.org/dc/terms/identifier"doi:10.1038/ncb2580"xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Jia J."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Fan Y."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Gong Y."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Willard B."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Fox P.L."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Arif A."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Horowitz A."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Penn M.S."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Graham L.M."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/author"Eswarappa S.M."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/pages"1046-1056"xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/title"Stimulus-dependent phosphorylation of profilin-1 in angiogenesis."xsd:string
http://purl.uniprot.org/citations/23000962http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/23000962http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23000962
http://purl.uniprot.org/citations/23000962http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23000962
http://purl.uniprot.org/uniprot/#_B1ARA9-mappedCitation-23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23000962
http://purl.uniprot.org/uniprot/#_B1ARB3-mappedCitation-23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23000962
http://purl.uniprot.org/uniprot/#_J3QMC2-mappedCitation-23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23000962
http://purl.uniprot.org/uniprot/#_P07737-mappedCitation-23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23000962
http://purl.uniprot.org/uniprot/#_Q8CAW4-mappedCitation-23000962http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23000962