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http://purl.uniprot.org/citations/7929237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7929237http://www.w3.org/2000/01/rdf-schema#comment"The type I adenylyl cyclase is directly stimulated by Ca2+ and calmodulin in vivo (Choi, E. J., Wong, S. T., Hinds, T. R. and Storm, D. R. (1992) J. Biol. Chem. 267, 12440-12442; Wu, Z., Wong, S. T., and Storm, D. R. (1993) J. Biol. Chem. 268, 23766-23768). In this study, we examined the sensitivity of the type I adenylyl cyclase expressed in HEK-293 cells to beta-adrenergic agonists or glucagon when intracellular Ca2+ was elevated by Ca2+ ionophore or carbachol. Although previous studies have shown that this enzyme can be directly stimulated by activated Gs in vitro, we demonstrate that it is not stimulated by Gs-coupled receptors in vivo. However, the enzyme was stimulated by Gs-coupled receptors in vivo when it was activated by intracellular Ca2+. For example, the Ca2+ ionophore A23187 stimulated the enzyme 3 +/-0.5-fold (n = 9) and isoproterenol alone did not stimulate the enzyme, but the combination of the two stimulated type I adenylyl cyclase 13 +/-2-fold (n = 9) in vivo. Similarly, 500 nM glucagon alone did not stimulate the enzyme but the combination of A23187 and glucagon activated the enzyme 90 +/-8-fold (n = 4). Synergistic stimulation of type I adenylyl cyclase activity was also obtained with combinations of carbachol and isoproterenol or glucagon. This phenomenon was not observed with a mutant enzyme that is insensitive to Ca2+ and calmodulin, suggesting that conformational changes caused by binding of calmodulin to the type I adenylyl cyclase enhance binding or coupling to activated Gs. These data illustrate that this adenylyl cyclase can couple Ca2+ and neurotransmitter signals to generate optimal cAMP levels, a property of the enzyme that may be important for its role in learning and memory in mammals."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(18)47263-8"xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Wu Z."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Storm D.R."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Wayman G.A."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Impey S."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Prichard L."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/author"Kindsvogel W."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/pages"25400-25405"xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/title"Synergistic activation of the type I adenylyl cyclase by Ca2+ and Gs-coupled receptors in vivo."xsd:string
http://purl.uniprot.org/citations/7929237http://purl.uniprot.org/core/volume"269"xsd:string
http://purl.uniprot.org/citations/7929237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7929237
http://purl.uniprot.org/citations/7929237http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7929237
http://purl.uniprot.org/uniprot/P01275#attribution-BCCF2A14DBAF942B7B122E09C5D3926Chttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/7929237