ArticleAmerican journal of physiology. Renal physiology2012
Multiple residues in the distal C terminus of the α-subunit have roles in modulating human epithelial sodium channel activity.
Article in American journal of physiology. Renal physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- The Epithelial Sodium Channel-An Underestimated Drug Target.International journal of molecular sciences · 2023Review
- Epithelial NaAnnual review of physiology · 2018Review
- Palmitate Stimulates the Epithelial Sodium Channel by Elevating Intracellular Calcium, Reactive Oxygen Species, and Phosphoinositide 3-Kinase Activity.Oxidative medicine and cellular longevity · 2018Article
- Specific Palmitoyltransferases Associate with and Activate the Epithelial Sodium Channel.The Journal of biological chemistry · 2017Article
- Human epithelial Na+ channel missense variants identified in the GenSalt study alter channel activity.American journal of physiology. Renal physiology · 2016Article
- Evaluation of the relationship between T663A polymorphism in the alpha-epithelial sodium channel gene and essential hypertension.Saudi medical journal · 2015Review
- Cysteine palmitoylation of the γ subunit has a dominant role in modulating activity of the epithelial sodium channel.The Journal of biological chemistry · 2014Article
- Blood pressure and amiloride-sensitive sodium channels in vascular and renal cells.Nature reviews. Nephrology · 2014Review
- Gain-of-function variant of the human epithelial sodium channel.American journal of physiology. Renal physiology · 2013Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Epithelial sodium channels (ENaC) are critically important in the regulation of ion and fluid balance in both renal and respiratory epithelia. ENaC functional polymorphisms may contribute to alterations in blood pressure in the general population. We previously reported that the A663T polymorphism in the C terminus of the α-subunit altered ENaC functional and surface expression in Xenopus laevis oocytes (Samaha FF, Rubenstein RC, Yan W, Ramkumar M, Levy DI, Ahn YJ, Sheng S, Kleyman TR. J Biol Chem 279: 23900-23907, 2004). We examined whether sites in the vicinity of 663 influenced channel activity by performing scanning Ala mutagenesis. Interestingly, only αT663/G667Aβγ channels exhibited increased currents compared with αT663βγ. This increase in channel activity reflected an increase in channel open probability and not an increase in channel surface expression. In contrast, decreases in channel activity were observed with both αT663/C664Aβγ and αT663/C664Mβγ channels. The decrease in functional expression of αT663/C664Mβγ channels correlated with decreased surface expression, suggesting that the αC664M mutation altered the intracellular trafficking of the channel. While cytoplasmic Cys residues may be modified by the addition of palmitate, we did not observe palmitoylation of αC664. Our results suggest that multiple residues in the distal part of the cytoplasmic C terminus have roles in modulating channel activity.
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