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http://purl.uniprot.org/citations/12529354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12529354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12529354http://www.w3.org/2000/01/rdf-schema#comment"Drosophila 14-3-3zeta (D14-3-3zeta) modulates the activity of the Slowpoke calcium-dependent potassium channel (dSlo) by interacting with the dSlo binding protein, Slob. We show here that D14-3-3zeta forms dimers in vitro. Site-directed mutations in its putative dimerization interface result in a dimerization-deficient form of D14-3-3zeta. Both the wild-type and dimerization-deficient forms of D14-3-3zeta bind to Slob with similar affinity and form complexes with dSlo. When dSlo and Slob are expressed in mammalian cells, the dSlo channel activity is similarly modulated by co-expression of either the wild-type or the dimerization-deficient form of D14-3-3zeta. In addition, dSlo is still modulated by wild-type D14-3-3zeta in the presence of a 14-3-3 mutant, which does not itself bind to Slob but forms heterodimers with the wild-type 14-3-3. These data, taken together, suggest that monomeric D14-3-3zeta is capable of modulating dSlo channel activity in this regulatory complex."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m211907200"xsd:string
http://purl.uniprot.org/citations/12529354http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m211907200"xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Fei H."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Fei H."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Levitan I.B."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Levitan I.B."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Murrey H."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Murrey H."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Reddy S."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Reddy S."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/author"Zhou Y."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/pages"10073-10080"xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/pages"10073-10080"xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/title"Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/title"Monomeric 14-3-3 protein is sufficient to modulate the activity of the Drosophila slowpoke calcium-dependent potassium channel."xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/volume"278"xsd:string
http://purl.uniprot.org/citations/12529354http://purl.uniprot.org/core/volume"278"xsd:string