ArticleThe Biochemical journal1998
Cell surface expression and biosynthesis of epithelial Na+ channels.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- N-linked glycans are required on epithelial NaAmerican journal of physiology. Renal physiology · 2018Article
- Lung disease phenotypes caused by overexpression of combinations of α-, β-, and γ-subunits of the epithelial sodium channel in mouse airways.American journal of physiology. Lung cellular and molecular physiology · 2018Article
- Regulation of the epithelial NaThe Journal of biological chemistry · 2017Article
- Delivery of ENaC siRNA to epithelial cells mediated by a targeted nanocomplex: a therapeutic strategy for cystic fibrosis.Scientific reports · 2017Article
- Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.The Biochemical journal · 2017Article
- Article
- Expression and purification of the alpha subunit of the epithelial sodium channel, ENaC.Protein expression and purification · 2016Article
- Sialic acid accelerates the electrophoretic velocity of injured dorsal root ganglion neurons.Neural regeneration research · 2015Article
- Scaffold protein connector enhancer of kinase suppressor of Ras isoform 3 (CNK3) coordinates assembly of a multiprotein epithelial sodium channel (ENaC)-regulatory complex.The Journal of biological chemistry · 2012Article
- Saccharomyces cerivisiae as a model system for kidney disease: what can yeast tell us about renal function?American journal of physiology. Renal physiology · 2011Article
- Regulation of epithelial sodium channel trafficking by ubiquitination.Proceedings of the American Thoracic Society · 2010Review
- Epithelial sodium channel regulated by differential composition of a signaling complex.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Nedd4-2 isoforms ubiquitinate individual epithelial sodium channel subunits and reduce surface expression and function of the epithelial sodium channel.American journal of physiology. Renal physiology · 2008Article
- Effects of butyrate on active sodium and chloride transport in rat and rabbit distal colon.The Journal of physiology · 2002Article
- Gating of amiloride-sensitive Na(+) channels: subunit-subunit interactions and inhibition by the cystic fibrosis transmembrane conductance regulator.Biophysical journal · 2000Article
- Functional domains within the degenerin/epithelial sodium channel (Deg/ENaC) superfamily of ion channels.The Journal of physiology · 1999Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The epithelial Na+ channel (ENaC) complex is composed of three homologous subunits: alpha, beta and gamma. Mutations in ENaC subunits can increase the number of channels on the cell surface, causing a hereditary form of hypertension called Liddle's syndrome, or can decrease channel activity, causing pseudohypoaldosteronism type I, a salt-wasting disease of infancy. To investigate surface expression, we studied ENaC subunits expressed in COS-7 and HEK293 cells. Using surface biotinylation and protease sensitivity, we found that when individual ENaC subunits are expressed alone, they traffic to the cell surface. The subunits are glycosylated with high-mannose oligosaccharides, but seem to have the carbohydrate removed before they reach the cell surface. Moreover, subunits form a complex that cannot be disrupted by several non-ionic detergents. The pattern of glycosylation and detergent solubility/insolubility persists when the N-teminal and C-terminal cytoplasmic regions of ENaC are removed. With co-expression of all three ENaC subunits, the insoluble complex is the predominant species. These results show that ENaC and its family members are unique in their trafficking, biochemical characteristics and post-translational modifications.
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