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http://purl.uniprot.org/citations/16125056http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16125056http://www.w3.org/2000/01/rdf-schema#comment"The Cbl protein functions both as a multivalent adaptor and a negative regulator of receptor tyrosine kinases (RTKs), the latter by directing polyubiquitination of RTKs. To study the function of Cbl in endothelial cell signalling and angiogenesis, wild-type Cbl and tyrosine kinase binding (TKB) domain mutated Cbl (G306E) were overexpressed in murine immortalised brain endothelial (IBE) cells. Wild-type Cbl cells exhibited enhanced proliferation in low serum compared with the control and G306E Cbl cells. Furthermore, up-regulated phosphorylation of fibroblast growth factor receptor 1 (FGFR-1) and Akt were observed in wild-type Cbl cells upon FGF-2 stimulation. A Cbl TKB domain mutant, G306E, disrupted the phosphorylation of the FGFR-1 but not that of FRS2. In the tubular morphogenesis assay, cells expressing wild-type Cbl initially formed tubular structures. These showed decreased stability and converted into cell aggregates, possibly due to a failure to cease proliferating. Our data support the idea that the wild-type Cbl cells exhibit enhanced proliferation, and thus lose their ability to differentiate appropriately. The present study reveals a role of the Cbl protein in FGF-2 dependent signalling in endothelial cells by its destabilisation of tubular structures."xsd:string
http://purl.uniprot.org/citations/16125056http://purl.org/dc/terms/identifier"doi:10.1016/j.cellsig.2005.03.005"xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/author"Lu L."xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/author"Welsh M."xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/author"Holmqvist K."xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/name"Cell Signal"xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/pages"1433-1438"xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/title"A role of the protein Cbl in FGF-2-induced angiogenesis in murine brain endothelial cells."xsd:string
http://purl.uniprot.org/citations/16125056http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/16125056http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16125056
http://purl.uniprot.org/citations/16125056http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16125056
http://purl.uniprot.org/uniprot/#_A0A0X1KG61-mappedCitation-16125056http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/#_B1NE42-mappedCitation-16125056http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/#_Q2M4H7-mappedCitation-16125056http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/#_P22682-mappedCitation-16125056http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/A0A0X1KG61http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/P22682http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/Q2M4H7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16125056
http://purl.uniprot.org/uniprot/B1NE42http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16125056