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http://purl.uniprot.org/citations/16556600http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16556600http://www.w3.org/2000/01/rdf-schema#comment"The N-terminal regulatory region of the high affinity cAMP-specific phosphodiesterase, PDE7A1, contains two copies of the cAMP-dependent kinase (PKA) pseudosubstrate site RRGAI. In betaTC3 insulinoma cells, PDE7A1 co-localizes with PKA II in the Golgi-centrosome region. The roles PDE7A1 and its regulatory region play in cAMP signaling were examined by studying interactions with PKA subunits. PDE7A1 associates with the dissociated C subunit of PKA (C), but does not bind tetrameric PKA holoenzyme. High affinity binding of C by PDE7A1 inhibits kinase activity in vitro (IC50 = 0.5 nm). The domain containing PKA pseudosubstrate sites at the N terminus of PDE7A1 mediates complex formation with C. The PDE7A1 N-terminal repeat region inhibits C activity in CHO-K1 cells and also suppresses C dependent, cAMP-independent, physiological responses in yeast. Thus, PDE7A1 possesses a non-catalytic activity that can contribute to the termination of cAMP signals via direct inhibition of C. This study identifies a novel inhibitor of PKA and a non-catalytic affect of a cyclic nucleotide phosphodiesterase."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m601333200"xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/author"Han P."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/author"Michaeli T."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/author"Rubin C."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/author"Sonati P."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/pages"15050-15057"xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/title"PDE7A1, a cAMP-specific phosphodiesterase, inhibits cAMP-dependent protein kinase by a direct interaction with C."xsd:string
http://purl.uniprot.org/citations/16556600http://purl.uniprot.org/core/volume"281"xsd:string
http://purl.uniprot.org/citations/16556600http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16556600
http://purl.uniprot.org/citations/16556600http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16556600
http://purl.uniprot.org/uniprot/#_P70453-mappedCitation-16556600http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/#_P06776-mappedCitation-16556600http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/#_Q3U3Y7-mappedCitation-16556600http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/#_Q6P5G2-mappedCitation-16556600http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/P06776http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/Q6P5G2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/P70453http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16556600
http://purl.uniprot.org/uniprot/Q3U3Y7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16556600