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http://purl.uniprot.org/citations/20657592http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20657592http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20657592http://www.w3.org/2000/01/rdf-schema#comment"The endocannabinoid 2-arachidonoylglycerol (2-AG) regulates neurotransmission and neuroinflammation by activating CB1 cannabinoid receptors on neurons and CB2 cannabinoid receptors on microglia. Enzymes that hydrolyze 2-AG, such as monoacylglycerol lipase, regulate the accumulation and efficacy of 2-AG at cannabinoid receptors. We found that the recently described serine hydrolase alpha-beta-hydrolase domain 6 (ABHD6) also controls the accumulation and efficacy of 2-AG at cannabinoid receptors. In cells from the BV-2 microglia cell line, ABHD6 knockdown reduced hydrolysis of 2-AG and increased the efficacy with which 2-AG can stimulate CB2-mediated cell migration. ABHD6 was expressed by neurons in primary culture and its inhibition led to activity-dependent accumulation of 2-AG. In adult mouse cortex, ABHD6 was located postsynaptically and its selective inhibition allowed the induction of CB1-dependent long-term depression by otherwise subthreshold stimulation. Our results indicate that ABHD6 is a rate-limiting step of 2-AG signaling and is therefore a bona fide member of the endocannabinoid signaling system."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.org/dc/terms/identifier"doi:10.1038/nn.2601"xsd:string
http://purl.uniprot.org/citations/20657592http://purl.org/dc/terms/identifier"doi:10.1038/nn.2601"xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Li W."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Xu C."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Xu C."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Lin Y.H."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Lin Y.H."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Alexander J.P."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Alexander J.P."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Blankman J.L."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Blankman J.L."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Bodor A.L."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Bodor A.L."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Coy J."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Coy J."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Cravatt B.F."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Cravatt B.F."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Fung S."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Fung S."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Horne E.A."xsd:string
http://purl.uniprot.org/citations/20657592http://purl.uniprot.org/core/author"Horne E.A."xsd:string