| http://purl.uniprot.org/citations/12223484 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12223484 | http://www.w3.org/2000/01/rdf-schema#comment | "Recently, several studies have reported oligomerization of G protein-coupled receptors, although the functional implications of this phenomenon are still unclear. Using fluorescence resonance energy transfer (FRET) and coimmunoprecipitation (COIP), we previously reported that the human thyrotropin (TSH) receptor tagged with green fluorescent protein (TSHR(GFP)) and expressed in a heterologous system was present as oligomeric complexes on the cell surface. Here, we have extended this biophysical and biochemical approach to study the regulation of such oligomeric complexes. Co-expression of TSHR(GFP) and TSHR(Myc) constructs in Chinese hamster ovary cells resulted in FRET-positive cells. The specificity of the FRET signal was verified by the absence of energy transfer in individually transfected TSHR(GFP) and TSHR(Myc):Cy3 cells cultured together and also by acceptor photobleaching. Occupation of the receptor molecule by the ligand (TSH) resulted in a dose-dependent decrease in the FRET index from 20% in the absence of TSH to <1% with 10(3) microunits/ml of TSH. Such reduction in oligomeric forms was also confirmed by coimmunoprecipitation. Exposure of TSHR(GFP/Myc) cells to forskolin or cytochalasin D caused no change in the FRET index, confirming that the decrease in the oligomeric complexes was a receptor-dependent phenomenon and free of energy or microtuble requirements. The TSH-induced decrease in TSHR oligomers was found to be secondary to dissociation of the TSHR complexes as evidenced by an increase in fluorescent intensity of photobleached spots of GFP fluorescence with 10(3) microunits/ml of TSH. These data indicated that the less active conformation of the TSHR was comprised of receptor complexes and that such complexes were dissociated on the binding of ligand. Such observations support the concept of a constitutively active TSHR dimer or monomer that is naturally inhibited by the formation of higher order complexes. Inhibition of these oligomeric forms by ligand binding returns the TSHR to an activated state."xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m206693200"xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/author | "Graves P."xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/author | "Davies T.F."xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/author | "Latif R."xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/pages | "45059-45067"xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/title | "Ligand-dependent inhibition of oligomerization at the human thyrotropin receptor."xsd:string |
| http://purl.uniprot.org/citations/12223484 | http://purl.uniprot.org/core/volume | "277"xsd:string |
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