| http://purl.uniprot.org/citations/16030140 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16030140 | http://www.w3.org/2000/01/rdf-schema#comment | "The co-repressor proteins SMRT and NCoR concentrate in specific subnuclear compartments and function with DNA-binding factors to inhibit transcription. To provide detailed mechanistic understanding of these activities, this study tested the hypothesis that functional interactions with transcription factors, such as the pituitary-gland-specific Pit-1 homeodomain protein, direct the subnuclear organization and activity of co-repressor complexes. Both SMRT and NCoR repressed Pit-1-dependent transcription, and NCoR was co-immunoprecipitated with Pit-1. Immunofluorescence experiments confirmed that endogenous NCoR is concentrated in small focal bodies and that incremental increases in fluorescent-protein-tagged NCoR expression lead to progressive increases in the size of these structures. In pituitary cells, the endogenous NCoR localized with endogenous Pit-1 and the co-expression of a fluorescent-protein-labeled Pit-1 redistributed both NCoR and SMRT into diffuse nucleoplasmic compartments that also contained histone deacetylase and chromatin. Automated image-analysis methods were applied to cell populations to characterize the reorganization of co-repressor proteins by Pit-1 and mutation analysis showed that Pit-1 DNA-binding activity was necessary for the reorganization of co-repressor proteins. These data support the hypothesis that spherical foci serve as co-repressor storage compartments, whereas Pit-1/co-repressor complexes interact with target genes in more widely dispersed subnuclear domains. The redistribution of co-repressor complexes by Pit-1 might represent an important mechanism by which transcription factors direct changes in cell-specific gene expression."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.org/dc/terms/identifier | "doi:10.1242/jcs.02450"xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/author | "Voss T.C."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/author | "Day R.N."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/author | "Booker C.F."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/author | "Demarco I.A."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/name | "J Cell Sci"xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/pages | "3277-3288"xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/title | "Functional interactions with Pit-1 reorganize co-repressor complexes in the living cell nucleus."xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://purl.uniprot.org/core/volume | "118"xsd:string |
| http://purl.uniprot.org/citations/16030140 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16030140 |
| http://purl.uniprot.org/citations/16030140 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/16030140 |
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