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http://purl.uniprot.org/citations/25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25420509http://www.w3.org/2000/01/rdf-schema#comment"The two-pore domain potassium (K2P) channels TASK-1 (KCNK3) and TASK-3 (KCNK9) are important determinants of background K(+) conductance and membrane potential. TASK-1/3 activity is regulated by hormones and transmitters that act through G protein-coupled receptors (GPCR) signalling via G proteins of the Gαq/11 subclass. How the receptors inhibit channel activity has remained unclear. Here, we show that TASK-1 and -3 channels are gated by diacylglycerol (DAG). Receptor-initiated inhibition of TASK required the activity of phospholipase C, but neither depletion of the PLC substrate PI(4,5)P2 nor release of the downstream messengers IP3 and Ca(2+). Attenuation of cellular DAG transients by DAG kinase or lipase suppressed receptor-dependent inhibition, showing that the increase in cellular DAG-but not in downstream lipid metabolites-mediates channel inhibition. The findings identify DAG as the signal regulating TASK channels downstream of GPCRs and define a novel role for DAG that directly links cellular DAG dynamics to excitability."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.org/dc/terms/identifier"doi:10.1038/ncomms6540"xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Oliver D."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Lindner M."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Albus A."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Leitner M.G."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Bunemann M."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Greifenberg L."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Kronimus Y."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/author"Wilke B.U."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/pages"5540"xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/title"Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors."xsd:string
http://purl.uniprot.org/citations/25420509http://purl.uniprot.org/core/volume"5"xsd:string
http://purl.uniprot.org/citations/25420509http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25420509
http://purl.uniprot.org/citations/25420509http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25420509
http://purl.uniprot.org/uniprot/#_A0A024R240-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_A0A6H1Z4W8-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_B9EIJ4-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_B7Z581-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_G9FP35-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_G9FP37-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509
http://purl.uniprot.org/uniprot/#_G9FP38-mappedCitation-25420509http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25420509