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http://purl.uniprot.org/citations/8621381http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8621381http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8621381http://www.w3.org/2000/01/rdf-schema#comment"The heterodimeric karyopherin functions in targeting a nuclear localization sequence (NLS)-containing protein to the nuclear pore complex followed by Ran-GTP and p10-mediated translocation of the NLS protein into the nucleoplasm. It was shown recently that Ran-GTP dissociated the karyopherin heterodimer and, in doing so, associated with karyopherin beta (Rexach, M., and Blobel, G. (1995) Cell 83, 683-692). We show here, using all recombinant yeast proteins expressed in Escherichia coli, that karyopherin beta binds to Ran-GTP and inhibits GTP hydrolysis stimulated by RanGAP (the Ran-specific GTPase activating protein). Inhibition of RanGAP-stimulated GTP hydrolysis by karyopherin beta was dependent on karyopherin beta concentration relative to Ran-GTP. Complete inhibition of RanGAP was observed at karyopherin beta concentrations that were equimolar to Ran-GTP. In gel filtration experiments, we found Ran-GTP and karyopherin beta to form a stoichiometric complex. Ran-GDP bound only weakly to karyopherin beta. We propose that stoichiometric complex formation between karyopherin beta and Ran-GTP renders Ran-GTP inaccessible to RanGAP."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.10.5313"xsd:string
http://purl.uniprot.org/citations/8621381http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.10.5313"xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/author"Blobel G."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/author"Blobel G."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/author"Floer M."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/author"Floer M."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/pages"5313-5316"xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/pages"5313-5316"xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/title"The nuclear transport factor karyopherin beta binds stoichiometrically to Ran-GTP and inhibits the Ran GTPase activating protein."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/title"The nuclear transport factor karyopherin beta binds stoichiometrically to Ran-GTP and inhibits the Ran GTPase activating protein."xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8621381http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8621381http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8621381
http://purl.uniprot.org/citations/8621381http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8621381
http://purl.uniprot.org/citations/8621381http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8621381
http://purl.uniprot.org/citations/8621381http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8621381
http://purl.uniprot.org/uniprot/Q06142http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8621381
http://purl.uniprot.org/uniprot/Q06142#attribution-950B1EF3B42BC60AB278F7BA65523C62http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8621381