RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10518933http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10518933http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10518933http://www.w3.org/2000/01/rdf-schema#comment"Recently, we have shown that the delta subunit of the cGMP phosphodiesterase (PDE delta) interacts with the retinitis pigmentosa guanine regulator (RPGR). Here, using the two-hybrid system, we identify a member of the Arf-like protein family of Ras-related GTP-binding proteins, Arl3, that interacts with PDE delta. The interaction was verified by fluorescence spectroscopy and co-immunoprecipitation. Arl3 features an unusually low affinity for guanine nucleotides, with a KD of 24 nM for GDP and 48 microM for GTP. Fluorescence spectroscopy shows that PDE delta binds and specifically stabilizes the GTP-bound form of Arl3 by strongly decreasing the dissociation rate of GTP. Thus, PDE delta is an effector of Arl3 and could provide a novel nucleotide exchange mechanism by which PDE delta stabilizes Arl3 in its active GTP-bound form."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(99)01117-5"xsd:string
http://purl.uniprot.org/citations/10518933http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(99)01117-5"xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Becker J."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Becker J."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Hanzal-Bayer M."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Hanzal-Bayer M."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Linari M."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/author"Linari M."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/pages"55-59"xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/pages"55-59"xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/title"The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/title"The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner."xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/volume"458"xsd:string
http://purl.uniprot.org/citations/10518933http://purl.uniprot.org/core/volume"458"xsd:string
http://purl.uniprot.org/citations/10518933http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10518933
http://purl.uniprot.org/citations/10518933http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10518933
http://purl.uniprot.org/citations/10518933http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10518933
http://purl.uniprot.org/citations/10518933http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10518933