| pubmed-article:12006486 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12006486 | lifeskim:mentions | umls-concept:C0751283 | lld:lifeskim |
| pubmed-article:12006486 | lifeskim:mentions | umls-concept:C0528200 | lld:lifeskim |
| pubmed-article:12006486 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:12006486 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
| pubmed-article:12006486 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:12006486 | pubmed:dateCreated | 2002-5-13 | lld:pubmed |
| pubmed-article:12006486 | pubmed:abstractText | Membrane-bound receptors such as tyrosine kinases and ionotropic receptors are associated with large protein networks structured by protein-protein interactions involving multidomain proteins. Although these networks have emerged as a general mechanism of cellular signalling, much less is known about the protein complexes associated with G-protein-coupled receptors (GPCRs). Using a proteomic approach based on peptide affinity chromatography followed by mass spectrometry and immunoblotting, we have identified 15 proteins that interact with the C- terminal tail of the 5-hydroxytryptamine 2C (5-HT(2C)) receptor, a GPCR. These proteins include several synaptic multidomain proteins containing one or several PDZ domains (PSD95 and the proteins of the tripartite complex Veli3-CASK-Mint1), proteins of the actin/spectrin cytoskeleton and signalling proteins. Coimmunoprecipitation experiments showed that 5-HT(2C) receptors interact with PSD95 and the Veli3-CASK-Mint1 complex in vivo. Electron microscopy also indicated a synaptic enrichment of Veli3 and 5-HT(2C) receptors and their colocalization in microvilli of choroidal cells. These results indicate that the 5-HT(2C) receptor is associated with protein networks that are important for its synaptic localization and its coupling to the signalling machinery. | lld:pubmed |
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| pubmed-article:12006486 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12006486 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12006486 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12006486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12006486 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12006486 | pubmed:month | May | lld:pubmed |
| pubmed-article:12006486 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:DumuisAlineA | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:AlonsoGérardG | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:BockaertJoëlJ | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:BécamelCarine... | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:MarinPhilippe... | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:GaléottiNatha... | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:DemeyEmmanuel... | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:JouinPatrickP | lld:pubmed |
| pubmed-article:12006486 | pubmed:author | pubmed-author:UllmerChristo... | lld:pubmed |
| pubmed-article:12006486 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12006486 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:12006486 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:12006486 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12006486 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12006486 | pubmed:pagination | 2332-42 | lld:pubmed |
| pubmed-article:12006486 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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