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http://purl.uniprot.org/citations/19346499http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19346499http://www.w3.org/2000/01/rdf-schema#comment"Adhesion and motility of mammalian leukocytes are essential requirements for innate and adaptive immune defense mechanisms. We show here that the guanine nucleotide exchange factor cytohesin-1, which had previously been demonstrated to be an important component of beta-2 integrin activation in lymphocytes, regulates the activation of the small GTPase RhoA in primary dendritic cells (DCs). Cytohesin-1 and RhoA are both required for the induction of chemokine-dependent conformational changes of the integrin beta-2 subunit of DCs during adhesion under physiological flow conditions. Furthermore, use of RNAi in murine bone marrow DCs (BM-DCs) revealed that interference with cytohesin-1 signaling impairs migration of wild-type dendritic cells in complex 3D environments and in vivo. This phenotype was not observed in the complete absence of integrins. We thus demonstrate an essential role of cytohesin-1/RhoA during ameboid migration in the presence of integrins and further suggest that DCs without integrins switch to a different migration mode."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.org/dc/terms/identifier"doi:10.1182/blood-2008-08-176123"xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Weber C."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Alon R."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Schild C."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Kolanus W."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Sixt M."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Fraemohs L."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Grell J."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Forster R."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Quast T."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Czeloth N."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Lammermann T."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Dreck K."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/author"Tappertzhofen B."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/name"Blood"xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/pages"5801-5810"xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/title"Cytohesin-1 controls the activation of RhoA and modulates integrin-dependent adhesion and migration of dendritic cells."xsd:string
http://purl.uniprot.org/citations/19346499http://purl.uniprot.org/core/volume"113"xsd:string
http://purl.uniprot.org/citations/19346499http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19346499
http://purl.uniprot.org/citations/19346499http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19346499
http://purl.uniprot.org/uniprot/#_A0A0A6YWJ1-mappedCitation-19346499http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19346499
http://purl.uniprot.org/uniprot/#_A0A0A6YXF6-mappedCitation-19346499http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19346499