| http://purl.uniprot.org/citations/10419536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10419536 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10419536 | http://www.w3.org/2000/01/rdf-schema#comment | "The ubiquitous intracellular Ca(2+) sensor calmodulin (CaM) regulates numerous proteins involved in cellular signaling of G protein-coupled receptors, but most known interactions between GPCRs and CaM occur downstream of the receptor. Using a sequence-based motif search, we have identified the third intracellular loop of the opioid receptor family as a possible direct contact point for interaction with CaM, in addition to its established role in G protein activation. Peptides derived from the third intracellular loop of the mu-opioid (OP(3)) receptor strongly bound CaM and were able to reduce binding interactions observed between CaM and immunopurified OP(3) receptor. Functionally, CaM reduced basal and agonist-stimulated (35)S-labeled guanosine 5'-3-O-(thio)triphosphate incorporation, a measure of G protein activation, in membranes containing recombinant OP(3) receptor. Changes in CaM membrane levels as a result of overexpression or antisense CaM suppression inversely affected basal and agonist-induced G protein activation. The ability of CaM to abolish high affinity binding sites of an agonist at OP(3) further supports the hypothesis of a direct interaction between CaM and opioid receptors. An OP(3) receptor mutant with a Lys(273) --> Ala substitution (K273A-OP(3)), an amino acid predicted to play a critical role in CaM binding based on motif structure, was found to be unaffected by changes in CaM levels but coupled more efficiently to G proteins than the wild-type receptor. Stimulation of both the OP(1) (delta-opioid) and OP(3) wild-type receptors, but not the K273A-OP(3) mutant, induced release of CaM from the plasma membrane. These results suggest that CaM directly competes with G proteins for binding to opioid receptors and that CaM may itself serve as an independent second messenger molecule that is released upon receptor stimulation."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.31.22081"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.31.22081"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Wang D."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Sadee W."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Sadee W."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Quillan J.M."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/author | "Quillan J.M."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/pages | "22081-22088"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/pages | "22081-22088"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/title | "Calmodulin binding to G protein-coupling domain of opioid receptors."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/title | "Calmodulin binding to G protein-coupling domain of opioid receptors."xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10419536 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10419536 |
| http://purl.uniprot.org/citations/10419536 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10419536 |
| http://purl.uniprot.org/citations/10419536 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10419536 |
| http://purl.uniprot.org/citations/10419536 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10419536 |