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http://purl.uniprot.org/citations/16815842http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16815842http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16815842http://www.w3.org/2000/01/rdf-schema#comment"ErbB-4 is cleaved by alpha- and gamma-secretases to release a soluble 80-kDa intracellular domain, termed s80, which translocates to the nucleus. s80 is present in the nucleus of normal and cancerous mammary cells and is predicted to have a role in cell differentiation. To further investigate the mechanism by which s80 may mediate differentiation, we tested whether s80 regulates Eto2, a transcriptional corepressor that is involved in erythrocyte differentiation and is also implicated in human breast cancer. Here we show that ligand binding to ErbB-4 causes s80 translocation to the nucleus, where it colocalizes and interacts with Eto2. Expression of s80 blocks Eto2-mediated transcriptional repression of a heterologous promoter. This effect on Eto2 does not require s80 kinase activity and is mediated by the carboxyl-terminal region of s80. Although other cell surface receptors regulate transcription by activating signal transduction cascades, these data present a novel mechanism of corepressor regulation and suggest a role for Eto2 in ErbB-4-dependent differentiation."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m603998200"xsd:string
http://purl.uniprot.org/citations/16815842http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m603998200"xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/author"Carpenter G."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/author"Carpenter G."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/author"Linggi B."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/author"Linggi B."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/pages"25373-25380"xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/pages"25373-25380"xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/title"ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/title"ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional repression."xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16815842http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16815842http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16815842
http://purl.uniprot.org/citations/16815842http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16815842
http://purl.uniprot.org/citations/16815842http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16815842
http://purl.uniprot.org/citations/16815842http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16815842
http://purl.uniprot.org/uniprot/Q61527http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16815842
http://purl.uniprot.org/uniprot/O75081http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/16815842