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A postsynaptic neuron usually receives numerous impulses from several other presynaptic neurons. The axon hillock of the postsynaptic neuron integrates all these signals and determines the likelihood of firing an action potential.
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Related Experiment Video

Updated: Aug 14, 2025

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

Extracellular intersubunit interactions modulate epithelial Na⁺ channel gating.

Lei Zhang¹, Xueqi Wang¹, Jingxin Chen²

¹Departments of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania, USA; Department of Nephrology, Hunan Key Laboratory of Kidney Disease and Blood Purification, The Second Xiangya Hospital, Central South University, Changsha, Hunan, China; The Third Xiangya Hospital, Central South University, Changsha, Hunan, China.

The Journal of Biological Chemistry

|January 17, 2023

Summary

This summary is machine-generated.

Researchers identified specific subunit interactions in Epithelial Sodium Channels (ENaCs) that act as microswitches. Modulating these contacts with disulfide bonds alters ENaC activity and sodium ion self-inhibition.

Keywords:

Allosteric regulation Amiloride Channel gating Disulfide Epithelial sodium channel Extracellular domain Hydrogen peroxide Protein crosslinking Protein domain Protein–protein interaction Voltage clamp

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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

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Related Experiment Videos

Last Updated: Aug 14, 2025

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

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

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Area of Science:

Molecular biology
Biophysics
Ion channel function

Background:

Epithelial Sodium Channels (ENaCs) possess large extracellular domains crucial for activity regulation.
Extracellular structural changes influencing ENaC activity remain incompletely understood.

Purpose of the Study:

To define extracellular structural transitions linked to ENaC activity modulation.
To identify specific intersubunit contacts that regulate ENaC gating.

Main Methods:

Utilized Xenopus oocytes for functional expression of mouse ENaC.
Employed cysteine crosslinking to probe intersubunit contacts.
Assessed channel activity using two-electrode voltage clamp.

Main Results:

Disulfide bond formation between βE499C and αN510C (palm domains) activated ENaC.
Crosslinking βE499C with αQ441C (α-subunit thumb domain) inhibited ENaC.
Crosslinking αE557C (palm) and γQ398C (thumb) also strongly inhibited ENaC activity.

Conclusions:

Specific residue pairs at subunit interfaces function as microswitches.
These microswitches transmit conformational changes during ENaC gating and regulation.
Mechanisms altering Na+ self-inhibition were elucidated through distinct crosslinking strategies.