Source:http://linkedlifedata.com/resource/pubmed/id/17164241
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2007-2-12
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pubmed:abstractText |
The nucleus is an extremely dynamic compartment, and protein mobility represents a key factor in transcriptional regulation. We showed in a previous study that the diffusion of peroxisome proliferator-activated receptors (PPARs), a family of nuclear receptors regulating major cellular and metabolic functions, is modulated by ligand binding. In this study, we combine fluorescence correlation spectroscopy, dual color fluorescence cross-correlation microscopy, and fluorescence resonance energy transfer to dissect the molecular mechanisms controlling PPAR mobility and transcriptional activity in living cells. First, we bring new evidence that in vivo a high percentage of PPARs and retinoid X receptors is associated even in the absence of ligand. Second, we demonstrate that coregulator recruitment (and not DNA binding) plays a crucial role in receptor mobility, suggesting that transcriptional complexes are formed prior to promoter binding. In addition, association with coactivators in the absence of a ligand in living cells, both through the N-terminal AB domain and the AF-2 function of the ligand binding domain, provides a molecular basis to explain PPAR constitutive activity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
282
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4417-26
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pubmed:dateRevised |
2011-7-8
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pubmed:meshHeading |
pubmed-meshheading:17164241-Animals,
pubmed-meshheading:17164241-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:17164241-HeLa Cells,
pubmed-meshheading:17164241-Humans,
pubmed-meshheading:17164241-Ligands,
pubmed-meshheading:17164241-Nuclear Proteins,
pubmed-meshheading:17164241-Peroxisome Proliferator-Activated Receptors,
pubmed-meshheading:17164241-Protein Structure, Tertiary,
pubmed-meshheading:17164241-Protein Transport,
pubmed-meshheading:17164241-Retinoid X Receptors
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pubmed:year |
2007
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pubmed:articleTitle |
Association with coregulators is the major determinant governing peroxisome proliferator-activated receptor mobility in living cells.
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pubmed:affiliation |
Laboratory of Biomolecular Dynamics, Katholieke Universiteit, Leuven B-3001, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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