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http://purl.uniprot.org/citations/22240728http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22240728http://www.w3.org/2000/01/rdf-schema#comment"Protein-protein interactions define specificity in signal transduction and these interactions are central to transmembrane signaling by G-protein-coupled receptors (GPCRs). It is not quite clear, however, whether GPCRs and the regulatory trimeric G-proteins behave as freely and independently diffusible molecules in the plasma membrane or whether they form some preassociated complexes. Here we used clear-native polyacrylamide gel electrophoresis (CN-PAGE) to investigate the presumed coupling between thyrotropin-releasing hormone (TRH) receptor and its cognate G(q/11) protein in HEK293 cells expressing high levels of these proteins. Under different solubilization conditions, the TRH receptor (TRH-R) was identified to form a putative pentameric complex composed of TRH-R homodimer and G(q/11) protein. The presumed association of TRH-R with G(q/11)α or Gβ proteins in plasma membranes was verified by RNAi experiments. After 10- or 30-min hormone treatment, TRH-R signaling complexes gradually dissociated with a concomitant release of receptor homodimers. These observations support the model in which GPCRs can be coupled to trimeric G-proteins in preassembled signaling complexes, which might be dynamically regulated upon receptor activation. The precoupling of receptors with their cognate G-proteins can contribute to faster G-protein activation and subsequent signal transfer into the cell interior."xsd:string
http://purl.uniprot.org/citations/22240728http://purl.org/dc/terms/identifier"doi:10.1247/csf.11024"xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/author"Novotny J."xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/author"Drastichova Z."xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/name"Cell Struct Funct"xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/pages"1-12"xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/title"Identification of a preassembled TRH receptor-G(q/11) protein complex in HEK293 cells."xsd:string
http://purl.uniprot.org/citations/22240728http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/22240728http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22240728
http://purl.uniprot.org/citations/22240728http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22240728
http://purl.uniprot.org/uniprot/#_P29992-mappedCitation-22240728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/#_P34981-mappedCitation-22240728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/#_Q659F3-mappedCitation-22240728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/#_Q59FM5-mappedCitation-22240728http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/Q659F3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/P34981http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/Q59FM5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22240728
http://purl.uniprot.org/uniprot/P29992http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22240728