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http://purl.uniprot.org/citations/16199866http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16199866http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16199866http://www.w3.org/2000/01/rdf-schema#comment"The activity of GATA factors is regulated, in part, at the level of protein-protein interactions. LIM domain proteins, first defined by the zinc finger motifs found in the Lin11, Isl-1, and Mec-3 proteins, act as coactivators of GATA function in both hematopoietic and cardiovascular tissues. We have identified a novel GATA-LIM interaction between GATA6 and LMCD1/dyxin. The LIM domains and cysteine-rich domains in LMCD1/dyxin and the carboxy-terminal zinc finger of GATA6 mediate this interaction. Expression of LMCD1/dyxin is remarkably similar to that of GATA6, with high-level expression observed in distal airway epithelium of the lung, vascular smooth muscle, and myocardium. In contrast to other GATA-LIM protein interactions, LMCD1/dyxin represses GATA6 activation of both lung and cardiac tissue-specific promoters. Electrophoretic mobility shift and chromatin immunoprecipitation assays show that LMCD1/dyxin represses GATA6 function by inhibiting GATA6 DNA binding. These data reveal an interaction between GATA6 and LMCD1/dyxin and demonstrate a novel mechanism through which LIM proteins can assert their role as transcriptional cofactors of GATA proteins."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.20.8864-8873.2005"xsd:string
http://purl.uniprot.org/citations/16199866http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.20.8864-8873.2005"xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Wang Z."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Lu M.M."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Lu M.M."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Morrisey E.E."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Morrisey E.E."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Rath N."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/author"Rath N."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/pages"8864-8873"xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/pages"8864-8873"xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/title"LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6 function by inhibiting DNA binding."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/title"LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6 function by inhibiting DNA binding."xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16199866http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16199866http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16199866
http://purl.uniprot.org/citations/16199866http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16199866