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http://purl.uniprot.org/citations/10906137http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10906137http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10906137http://www.w3.org/2000/01/rdf-schema#comment"Yeast two-hybrid techniques were used to identify possible effectors for the heterotrimeric G protein G(z) in human bone marrow cells. Eya2, a human homologue of the Drosophila Eya transcription co-activator, was identified. Eya2 interacts with activated Galpha(z) and at least one other member of the Galpha(i) family, Galpha(i2). Interactions were confirmed in mammalian two-hybrid and glutathione S-transferase fusion protein pull-down assays. Regions of Eya2-mediating interaction were mapped to the C-terminal Eya consensus domain. Eya2 is an intrinsically cytosolic protein that is translocated to the nucleus by members of the Six homeodomain-containing family of proteins. Activated Galpha(z) and Galpha(i2) prevent Eya2 translocation and inhibit Six/Eya2-mediated activation of a reporter gene controlled through the MEF3/TATA promoter. Although G proteins are known to regulate the activity of numerous transcription factors, this regulation is normally achieved indirectly via one or more intermediates. We show here a novel functional regulation of a co-activator directly by G protein subunits."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m004577200"xsd:string
http://purl.uniprot.org/citations/10906137http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m004577200"xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Fan X."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Fan X."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Brass L.F."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Brass L.F."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Maire P."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Maire P."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Poncz M."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Poncz M."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Manning D.R."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Manning D.R."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Spitz F."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/author"Spitz F."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/pages"32129-32134"xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/pages"32129-32134"xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/title"The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins."xsd:string
http://purl.uniprot.org/citations/10906137http://purl.uniprot.org/core/title"The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins."xsd:string