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http://purl.uniprot.org/citations/14688794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14688794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14688794http://www.w3.org/2000/01/rdf-schema#comment"Fibroblast growth factors (FGFs) signal through high-affinity tyrosine kinase receptors to regulate a diverse range of cellular processes, including cell growth, differentiation and migration, as well as cell death. Here we identify XFLRT3, a member of a leucine-rich-repeat transmembrane protein family, as a novel modulator of FGF signalling. XFLRT3 is co-expressed with FGFs, and its expression is both induced after activation and downregulated after inhibition of FGF signalling. In gain- and loss-of function experiments, FLRT3 and FLRT2 phenocopy FGF signalling in Xenopus laevis. XFLRT3 signalling results in phosphorylation of ERK and is blocked by MAPK phosphatase 1, but not by expression of a dominant-negative phosphatidyl inositol 3-OH kinase (PI(3)K) mutant. XFLRT3 interacts with FGF receptors (FGFRs) in co-immunoprecipitation experiments in vitro and in bioluminescence resonance energy transfer assays in vivo. The results indicate that XFLRT3 is a transmembrane modulator of FGF-MAP kinase signalling in vertebrates."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.org/dc/terms/identifier"doi:10.1038/ncb1082"xsd:string
http://purl.uniprot.org/citations/14688794http://purl.org/dc/terms/identifier"doi:10.1038/ncb1082"xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Delius H."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Delius H."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Pollet N."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Pollet N."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Niehrs C."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Niehrs C."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Bottcher R.T."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/author"Bottcher R.T."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/name"Nat. Cell Biol."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/pages"38-44"xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/pages"38-44"xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/title"The transmembrane protein XFLRT3 forms a complex with FGF receptors and promotes FGF signalling."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/title"The transmembrane protein XFLRT3 forms a complex with FGF receptors and promotes FGF signalling."xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/14688794http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/14688794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14688794
http://purl.uniprot.org/citations/14688794http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14688794