Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-7-13
pubmed:abstractText
LRH-1 (liver receptor homologue-1), a transcription factor and member of the nuclear receptor superfamily, regulates the expression of its target genes, which are involved in bile acid and cholesterol homoeostasis. However, the molecular mechanisms of transcriptional control by LRH-1 are not completely understood. Previously, we identified Ku80 and Ku70 as LRH-1-binding proteins and reported that they function as co-repressors. In the present study, we identified an additional LRH-1-binding protein, ILF3 (interleukin enhancer-binding factor 3). ILF3 formed a complex with LRH-1 and the other two nuclear receptor co-activators PRMT1 (protein arginine methyltransferase 1) and PGC-1? (peroxisome proliferator-activated receptor ? co-activator-1?). We demonstrated that ILF3, PRMT1 and PGC-1? were recruited to the promoter region of the LRH-1-regulated SHP (small heterodimer partner) gene, encoding one of the nuclear receptors. ILF3 enhanced SHP gene expression in co-operation with PRMT1 and PGC-1? through the C-terminal region of ILF3. In addition, we found that the small interfering RNA-mediated down-regulation of ILF3 expression led to a reduction in the occupancy of PGC-1? at the SHP promoter and SHP expression. Taken together, our results suggest that ILF3 functions as a novel LRH-1 co-activator by acting synergistically with PRMT1 and PGC-1?, thereby promoting LRH-1-dependent gene expression.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ILF3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/NR5A2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Factor 90 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PPARGC1A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/PRMT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Arginine..., http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/nuclear receptor subfamily 0...
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1470-8728
pubmed:author
pubmed:copyrightInfo
© The Authors Journal compilation © 2011 Biochemical Society
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
437
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
531-40
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Interleukin enhancer-binding factor 3 functions as a liver receptor homologue-1 co-activator in synergy with the nuclear receptor co-activators PRMT1 and PGC-1?.
pubmed:affiliation
Department of Molecular Biology, Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Nagoya, Aichi 467-8603, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't