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Related Concept Videos

Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
Non-gated Ion Channels01:24

Non-gated Ion Channels

Ion channels are specialized proteins on the plasma membrane that allow charged ions to pass down their electrochemical gradient. Their main function is to maintain the membrane potential which is critical for cell viability. These channels are either gated or non-gated and can transport more than a thousand ions within milliseconds for the cellular event to occur.
Compared to the gated ion channels, the non-gated channels, also known as leakage or passive channels, have no gating mechanism.
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

Voltage-gated ion channels are transmembrane proteins that open and close in response to changes in the membrane potential. They are present on the membranes of all electrically excitable cells such as neurons, heart, and muscle cells.
Generally, all voltage-gated ion channels have a 'voltage-sensing domain' that spans the lipid bilayer. The charged residues in the sensor move in response to the membrane potential changes that open the channel allowing ions movement. There are several types of...

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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
07:38

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

Published on: March 30, 2015

Multivalent ions control the transport through lysenin channels.

Daniel Fologea1, Eric Krueger, Redwan Al Faori

  • 1Department of Biological Sciences, University of Arkansas, Fayetteville, AR 72701, USA. dfologea@uark.edu

Biophysical Chemistry
|August 21, 2010
PubMed
Summary

Multivalent ions alter lysenin channel conductivity by inducing reversible sub-conducting states. This ion interaction with lysenin channels was effectively modeled as an absorption process.

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A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
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Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

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Last Updated: Jun 10, 2026

Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
07:38

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A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters

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Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
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Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

Area of Science:

  • Biophysics
  • Ion Channel Physiology
  • Membrane Biology

Background:

  • Lysenin channels are pore-forming proteins.
  • Understanding ion interactions with ion channels is crucial for cell function.
  • Planar lipid bilayer membranes are used to study channel properties.

Purpose of the Study:

  • To investigate the effect of different ions on lysenin channel conductance.
  • To characterize the interaction mechanism between multivalent ions and lysenin channels.

Main Methods:

  • Incorporation of lysenin channels into planar lipid bilayer membranes.
  • Electrophysiological recordings of single channel currents.
  • Analysis of ion concentration-dependent conductance changes.
  • Development and application of a theoretical absorption model.

Main Results:

  • Multivalent ions inhibit lysenin channel conductance in a concentration-dependent manner.
  • Specific ions induced reversible sub-conducting or closed states.
  • Ion charge and size influenced the observed channel states.
  • Experimental data showed good agreement with the proposed isothermal absorption model.

Conclusions:

  • Multivalent ions modulate lysenin channel activity through interactions dependent on ion properties.
  • A simple isothermal absorption model accurately describes divalent ion interactions with lysenin channels.
  • These findings contribute to the understanding of ion channel gating mechanisms.