| http://purl.uniprot.org/citations/12770839 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12770839 | http://www.w3.org/2000/01/rdf-schema#comment | "Epithelial sodium channels (ENaCs) are composed of three structurally related subunits that form a tetrameric channel. The Xenopus laevis oocyte expression system was used to identify regions within the ENaC alpha-subunit that confer a dominant negative phenotype on functional expression of alphabetagamma-ENaC to define domains that have a role in subunit-subunit interactions. Coexpression of full-length mouse alphabetagamma-ENaC with either 1) the alpha-subunit first membrane-spanning domain and short downstream hydrophobic domain (alpha-M1H1); 2) alpha-M1H1 and its downstream hydrophilic extracellular loop (alpha-M1H1-ECL); 3) the membrane-spanning domain of a control type 2 transmembrane protein (glutamyl transpeptidase; gamma-GT) fused to the alpha-ECL (gamma-GT-alpha-ECL); 4) the extracellular domain of a control type 1 transmembrane protein (Tac) fused to the alpha-subunit second membrane-spanning domain and short upstream hydrophobic domain (Tac-alpha-H2M2); or 5) the alpha-subunit cytoplasmic COOH terminus (alpha-Ct) significantly reduced amiloride-sensitive Na+ currents in X. laevis oocytes. Functional expression of Na+ channels was not inhibited when full-length alphabetagamma-ENaC was coexpressed with either 1) the alpha-ECL lacking a signal-anchor sequence, 2) alpha-M1H1 and alpha-Ct expressed as a fusion protein, 3) full-length gamma-GT, or 4) full-length Tac. Furthermore, the expression of ROMK channels was not inhibited when full-length ROMK was coexpressed with either alpha-M1H1-ECL or alpha-Ct. Full-length FLAG-tagged alpha-, beta-, or gamma-ENaC coimmunoprecipitated with myc-tagged alpha-M1H1-ECL, whereas wild-type gamma-GT did not. These data suggest that multiple sites within the alpha-subunit participate in subunit-subunit interactions that are required for proper assembly of the heterooligomeric ENaC complex."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajprenal.00095.2003"xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Hu B."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Sheng S."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Ahn Y.J."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Bruns J.B."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Hughey R.P."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/author | "Kleyman T.R."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/name | "Am J Physiol Renal Physiol"xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/pages | "F600-9"xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/title | "Multiple epithelial Na+ channel domains participate in subunit assembly."xsd:string |
| http://purl.uniprot.org/citations/12770839 | http://purl.uniprot.org/core/volume | "285"xsd:string |
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