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http://purl.uniprot.org/citations/8550628http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8550628http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8550628http://www.w3.org/2000/01/rdf-schema#comment"In response to changes in vascular homeostasis, endothelial cells secrete endothelin-1 (ET-1), which in turn regulates gene expression and phenotype in underlying vascular cells. We characterized a nuclear signaling cascade in which Src protein-tyrosine kinases link the ET-1 receptor to induction of c-fos transcription. A dominant negative SrcK-kinase mutant blocked ET-1-stimulated c-fos transcription. Expression of the COOH-terminal Src kinase (Csk), which represses Src kinases, also blocked induction of c-fos transcription by ET-1. Activation of the c-fos promoter by ET-1 required both the CArG DNA sequence of the c-fos serum response element and the Ca2+/cAMP response element. In contrast, Src-induced c-fos transcription required only the CArG cis-element, demonstrating a divergence in signals regulating c-fos transcription. Thus, Src kinases contribute to a nuclear signaling cascade linking an ET-1 receptor to the CArG element of the c-fos serum response element. A Src-based pathway might play a more general role to propagate ET-1 nuclear signals that regulate cell growth and development. In addition, these results point to a widening role for nonreceptor protein-tyrosine kinases in propagating signals from G protein-coupled receptors."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.1.77"xsd:string
http://purl.uniprot.org/citations/8550628http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.1.77"xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Wang Y."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Herman W.H."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Herman W.H."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Simonson M.S."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/author"Simonson M.S."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/pages"77-82"xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/pages"77-82"xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/title"Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/title"Nuclear signaling by endothelin-1 requires Src protein-tyrosine kinases."xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8550628http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8550628http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8550628
http://purl.uniprot.org/citations/8550628http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8550628
http://purl.uniprot.org/citations/8550628http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8550628
http://purl.uniprot.org/citations/8550628http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8550628