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http://purl.uniprot.org/citations/10570155http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10570155http://www.w3.org/2000/01/rdf-schema#comment"The ability of integrins to mediate cell attachment to extracellular matrices and to blood proteins is regulated from inside the cell. Increased ligand-binding activity of integrins is critical for platelet aggregation upon blood clotting and for leukocyte extravasation to inflamed tissues. Decreased adhesion is thought to promote tumor cell invasion. R-Ras, a small intracellular GTPase, regulates the binding of integrins to their ligands outside the cell. Here we show that the Eph receptor tyrosine kinase, EphB2, can control integrin activity through R-Ras. Cells in which EphB2 is activated become poorly adherent to substrates coated with integrin ligands, and a tyrosine residue in the R-Ras effector domain is phosphorylated. The R-Ras phosphorylation and loss of cell adhesion are causally related, because forced expression of an R-Ras variant resistant to phosphorylation at the critical site made cells unresponsive to the anti-adhesive effect of EphB2. This is an unusual regulatory pathway among the small GTPases. Reduced adhesiveness induced through the Eph/R-Ras pathway may explain the repulsive effect of the Eph receptors in axonal pathfinding and may facilitate tumor cell invasion and angiogenesis."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.org/dc/terms/identifier"doi:10.1073/pnas.96.24.13813"xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Wang B."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Ruoslahti E."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Zou J.X."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Pasquale E.B."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Zisch A.H."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/author"Kalo M.S."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/pages"13813-13818"xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/title"An Eph receptor regulates integrin activity through R-Ras."xsd:string
http://purl.uniprot.org/citations/10570155http://purl.uniprot.org/core/volume"96"xsd:string
http://purl.uniprot.org/citations/10570155http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10570155
http://purl.uniprot.org/citations/10570155http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10570155
http://purl.uniprot.org/uniprot/#_P10301-mappedCitation-10570155http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10570155
http://purl.uniprot.org/uniprot/P10301http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10570155