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Related Experiment Video

Updated: Jul 15, 2026

A Fluorescence-Based Assay of Membrane Potential for High-Throughput Functional Study of Two Endogenous Ion Channels in Two Epithelial Cell Lines

A Fluorescence-Based Assay of Membrane Potential for High-Throughput Functional Study of Two Endogenous Ion Channels in Two Epithelial Cell Lines

Published on: June 22, 2022

CFTR stabilizes ENaC at the plasma membrane.

C Lu¹, C Jiang, S Pribanic

¹Program in Cell Biology, The Hospital for Sick Children, and Biochemistry Department, University of Toronto, 555 University Ave, Toronto, Ontario, Canada M5G 1X8.

Journal of Cystic Fibrosis : Official Journal of the European Cystic Fibrosis Society

|April 17, 2007

Summary

Cystic fibrosis transmembrane conductance regulator (CFTR) surprisingly stabilizes epithelial sodium channel (ENaC) at the cell surface. This suggests CFTR impacts ENaC stability rather than just its opening.

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Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

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Last Updated: Jul 15, 2026

A Fluorescence-Based Assay of Membrane Potential for High-Throughput Functional Study of Two Endogenous Ion Channels in Two Epithelial Cell Lines

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Published on: June 22, 2022

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

Demonstration of Proteolytic Activation of the Epithelial Sodium Channel (ENaC) by Combining Current Measurements with Detection of Cleavage Fragments

Published on: July 5, 2014

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

Area of Science:

Cell Biology
Ion Channel Physiology
Molecular Medicine

Background:

Epithelial sodium channel (ENaC) activity is crucial for ion and fluid transport.
The cystic fibrosis transmembrane conductance regulator (CFTR) is known to modulate ENaC channel opening.
Previous understanding suggested CFTR primarily affects ENaC gating.

Purpose of the Study:

To investigate the effect of CFTR on ENaC stability at the plasma membrane.
To determine if CFTR influences ENaC cell-surface half-life.

Main Methods:

Generation of MDCK-I cell lines stably expressing ENaC alone or with CFTR.
Development of an assay to quantify ENaC cell-surface half-life.

Main Results:

Co-expression of CFTR with ENaC led to stabilization of ENaC at the plasma membrane.
CFTR significantly increased the cell-surface half-life of ENaC.

Conclusions:

CFTR plays a role in regulating ENaC stability at the cell surface.
The findings suggest CFTR's influence on ENaC extends beyond channel opening to membrane trafficking and stability.