| http://purl.uniprot.org/citations/18067919 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18067919 | http://www.w3.org/2000/01/rdf-schema#comment | "FOG-2 is a transcriptional co-regulator that is required for cardiac morphogenesis as mice deficient in this factor die during mid-gestation of cardiac malformations. FOG-2 interacts with GATA4 to attenuate GATA4-dependent gene expression. The first 12 amino acids of FOG-2 (the FOG Repression Motif) are necessary to mediate this repression. To determine the mechanism by which the FOG Repression Motif functions, we identified 7 polypeptides from rat cardiac nuclear extracts that co-purified with a GST-FOG-2 fusion protein. All proteins identified are members of the NuRD nucleosome remodeling complex. Using in vitro binding and co-immunoprecipitation assays, we demonstrate that Metastasis-Associated proteins (MTA)-1, 2 and 3 and Retinoblastoma binding proteins RbAp46 and RbAp48 interact with FOG-2, but not with a mutant form of FOG-2 that is unable to repress transcription. Furthermore, we define a novel domain located in the C-terminal portion of MTA-1 that mediates the FOG-2/MTA-1 interaction. We also demonstrate that knockdown of MTA protein expression dramatically impairs the ability of FOG-2 to repress GATA4 activity. Finally, we show that the zinc finger domain of MTA-1 is required for FOG-2-mediated transcriptional repression and that this domain interacts with RbAp46 and RbAp48 subunits of the NuRD complex. Together, these results demonstrate the importance of FOG-2/MTA/RbAp interactions for FOG-2-mediated transcriptional repression and further define the molecular interactions between the FOG Repression Motif and the NuRD complex."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.yjmcc.2007.10.023"xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Hong W."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Blobel G.A."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Samant S.A."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Svensson E.C."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Roche A.E."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/author | "Bassett B.J."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/name | "J Mol Cell Cardiol"xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/pages | "352-360"xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/title | "The zinc finger and C-terminal domains of MTA proteins are required for FOG-2-mediated transcriptional repression via the NuRD complex."xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/18067919 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18067919 |
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