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http://purl.uniprot.org/citations/18762272http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18762272http://www.w3.org/2000/01/rdf-schema#comment"Endothelial migration, early step in angiogenesis, is tightly regulated by the coordinated action of tyrosine kinases and tyrosine phosphatases. HD-PTP contributes to endothelial motility, since endothelial cells silencing HD-PTP after transfection with iRNA acquire a scattered and spindle-shaped phenotype and migrate faster than controls. Since (i) the proto-oncogene Src contributes to the regulation of cell motility and (ii) HD-PTP has a potential binding site for Src, we investigated whether an interplay exists between these two proteins. We found that Src binds HD-PTP and this interaction is enhanced after exposure to basic fibroblast growth factor. While HD-PTP does not modulate the levels of Src phosphorylation both in vitro and in vivo, we found that Src phosphorylates HD-PTP on tyrosine residues. Here we show for the first time that (i) HD-PTP has a tyrosine phosphatase activity; (ii) HD-PTP phosphorylation by Src inhibits its enzymatic activity. Interestingly, pharmacological and genetic inhibition of Src abrogates the migratory phenotype of endothelial cells silencing HD-PTP. On these bases, and because we have previously demonstrated that HD-PTP binds and dephosphorylates focal adhesion kinase (FAK), another crucial regulator of cell migration, we hypothesize that HD-PTP participates to the regulation of endothelial motility through its interactions with Src and FAK."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.org/dc/terms/identifier"doi:10.1016/j.biocel.2008.08.005"xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/author"Garcia-Manteiga J.M."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/author"Castiglioni S."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/author"Mariotti M."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/author"Beguinot L."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/author"Maier J.A."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/name"Int J Biochem Cell Biol"xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/pages"687-693"xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/title"HD-PTP inhibits endothelial migration through its interaction with Src."xsd:string
http://purl.uniprot.org/citations/18762272http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/18762272http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18762272
http://purl.uniprot.org/citations/18762272http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18762272
http://purl.uniprot.org/uniprot/#_B4DST5-mappedCitation-18762272http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/#_B4DJ12-mappedCitation-18762272http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/#_B4DJ21-mappedCitation-18762272http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/#_Q9H3S7-mappedCitation-18762272http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/B4DJ12http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/Q9H3S7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/B4DJ21http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18762272
http://purl.uniprot.org/uniprot/B4DST5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18762272