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http://purl.uniprot.org/citations/15234985http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15234985http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15234985http://www.w3.org/2000/01/rdf-schema#comment"Aldosterone-induced serum- and glucocorticoid-inducible kinase isoform 1 (SGK1) contributes to the regulation of the epithelial sodium channel (ENaC), the activity of which is critical for long term blood pressure control. Aldosterone-induced SGK1 is thought to enhance ENaC surface expression by phosphorylating Nedd4-2 and thereby preventing ENaC retrieval and degradation. In outside-out membrane patches of Xenopus laevis oocytes heterologously expressing ENaC, amiloride-sensitive ENaC currents were enhanced by phosphatase inhibitors and were dependent on cytosolic Mg(2+). This indicates that a kinase is involved in channel regulation. Indeed, recombinant constitutively active SGK1, included in the pipette solution, caused a sustained 2-to 3-fold increase of ENaC currents. Deletion of the C terminus of alphaENaC largely reduced the stimulatory effect of SGK1, whereas stimulation by SGK1 did not require the presence of the C termini of the beta- or gamma-subunits. Replacing the serine residue Ser(621) of the SGK1 consensus motif in the C terminus of the alpha-subunit by an alanine specifically abolished the stimulatory effect of SGK. Our findings indicate that SGK1 can stimulate ENaC activity independently of an inhibition of Nedd4-2-mediated channel retrieval. This defines a novel regulatory pathway likely to be relevant for aldosterone-induced stimulation of ENaC in vivo."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m403260200"xsd:string
http://purl.uniprot.org/citations/15234985http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m403260200"xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/author"Korbmacher C."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/author"Korbmacher C."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/author"Diakov A."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/author"Diakov A."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/pages"38134-38142"xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/pages"38134-38142"xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/title"A novel pathway of epithelial sodium channel activation involves a serum- and glucocorticoid-inducible kinase consensus motif in the C terminus of the channel's alpha-subunit."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/title"A novel pathway of epithelial sodium channel activation involves a serum- and glucocorticoid-inducible kinase consensus motif in the C terminus of the channel's alpha-subunit."xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15234985http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15234985http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15234985
http://purl.uniprot.org/citations/15234985http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15234985
http://purl.uniprot.org/citations/15234985http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15234985
http://purl.uniprot.org/citations/15234985http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15234985
http://purl.uniprot.org/uniprot/O00141http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/15234985
http://purl.uniprot.org/uniprot/P37089#attribution-B76CC60CC0B0893516B7CC022ABF5E1Ehttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15234985