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http://purl.uniprot.org/citations/17245118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17245118http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17245118http://www.w3.org/2000/01/rdf-schema#comment"A number of target genes for the tumor suppressor, p53, have been identified, however, the mechanisms that contribute to p53-dependent apoptosis remain to be fully elucidated. In a comprehensive screen for p53 target genes, we have identified Cytoplasmic FMR Interacting Protein 2 (CYFIP2) as a p53-inducible gene. Here we show that the CYFIP2 promoter contains a p53-responsive element that confers p53 binding as well as transcriptional activation of a heterologous reporter. Inducible expression of CYFIP2 is sufficient for caspase activation and cellular apoptosis, reminiscent of p53 activation. Together, these results suggest that CYFIP2 is a direct p53 target gene that may be part of a redundant network of genes responsible for p53-dependent apoptosis. In addition, the sensitivity of CYFIP2 protein subcellular localization to Leptomycin-B, a CRM-1/Exportin inhibitor, suggests that the biological functions of CYFIP2 may extend from the cytoplasmic compartment into the nucleus of the cell."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.org/dc/terms/identifier"doi:10.4161/cc.6.1.3665"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.org/dc/terms/identifier"doi:10.4161/cc.6.1.3665"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Liang P."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Liang P."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Stein S."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Stein S."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Cho Y.-J."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Cho Y.-J."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Jackson R.S. II"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/author"Jackson R.S. II"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/name"Cell Cycle"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/pages"95-103"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/pages"95-103"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/title"CYFIP2, a direct p53 target, is leptomycin-B sensitive."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/title"CYFIP2, a direct p53 target, is leptomycin-B sensitive."xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/17245118http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/17245118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17245118
http://purl.uniprot.org/citations/17245118http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17245118