Ivan Gautschi

TL;DR: The ion-selective permeability, the gating properties and the pharmacological profile of the channel formed by coexpressing the three subunits in oocytes are similar to that of the native channel.

TL;DR: It is shown that ENaC is a short‐lived protein that is ubiquitinated in vivo on the α and γ (but not β) subunits, and a paradigm for ubiquitination‐mediated regulation of ion channels is proposed.

TL;DR: A quantitative assay based on the binding of 125I-labeled M2 anti-FLAG monoclonal antibody directed against a FLAG reporter epitope introduced in the extracellular loop of each of the alpha, beta, and gamma ENaC subunits is developed, demonstrating that only heteromultimeric channels made of alpha, Beta, and Gamma ENac subunits are maximally and efficiently expressed at the cell surface.

TL;DR: In this article, the subunit stoichiometry of the epithelial sodium channel (ENaC) has been solved by quantitative analysis of cell surface expression of ENaC alpha, beta and gamma subunits.

TL;DR: Findings show that the three PY motifs in the C‐termini of ENaC are involved in the regulation of channel activity, probably via protein‐protein interactions, which is critical for the maintenance of normal Na re absorption in the kidney and of Na+ balance and blood pressure.