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http://purl.uniprot.org/citations/9545239http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9545239http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9545239http://www.w3.org/2000/01/rdf-schema#comment"Compartmentalization of protein kinases with substrates is a mechanism that may promote specificity of intracellular phosphorylation events. We have cloned a low-molecular weight A-kinase Anchoring Protein, called AKAP18, which targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. Membrane anchoring is mediated by the first 10 amino acids of AKAP18, and involves residues Gly1, Cys4 and Cys5 which are lipid-modified through myristoylation and dual palmitoylation, respectively. Transient transfection of AKAP18 into HEK-293 cells expressing the cardiac L-type Ca2+ channel promoted a 34 9% increase in cAMP-responsive Ca2+ currents. In contrast, a targeting-deficient mutant of AKAP18 had no effect on Ca2+ currents in response to the application of a cAMP analog. Further studies demonstrate that AKAP18 facilitates GLP-1-mediated insulin secretion in a pancreatic beta cell line (RINm5F), suggesting that membrane anchoring of the kinase participates in physiologically relevant cAMP-responsive events that may involve ion channel activation."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.8.2261"xsd:string
http://purl.uniprot.org/citations/9545239http://purl.org/dc/terms/identifier"doi:10.1093/emboj/17.8.2261"xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Dean R.A."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Dean R.A."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Scott J.D."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Scott J.D."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Lester L.B."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Lester L.B."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Langeberg L.K."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Langeberg L.K."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Fraser I.D.C."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Fraser I.D.C."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Marrion N.V."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Marrion N.V."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Tavalin S.J."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Tavalin S.J."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Westphal A.M."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/author"Westphal A.M."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/9545239http://purl.uniprot.org/core/name"EMBO J."xsd:string