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Related Concept Videos

Ion Channels01:19

Ion Channels

92.6K
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...
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Non-gated Ion Channels01:24

Non-gated Ion Channels

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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....
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Non-gated Ion Channels01:24

Non-gated Ion Channels

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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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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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Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

15.4K
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...
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Updated: Mar 26, 2026

Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)
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Monitoring Leucine-Rich Repeat Containing 8 Channel (LRRC8/VRAC) Activity Using Sensitized-Emission Förster Resonance Energy Transfer (SE-FRET)

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LRRC8 Proteins Form Volume-Regulated Anion Channels that Sense Ionic Strength.

Ruhma Syeda1, Zhaozhu Qiu2, Adrienne E Dubin1

  • 1Department of Molecular and Cellular Neuroscience, Howard Hughes Medical Institute, Dorris Neuroscience Center, The Scripps Research Institute, La Jolla, CA 92037, USA.

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|January 30, 2016
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The volume-regulated anion channel (VRAC) pore is formed by LRRC8 proteins. Hypotonic stress activates VRAC by decreasing cytoplasmic ionic strength, revealing the channel

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A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane
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Functional Characterization of Na+/H+ Exchangers of Intracellular Compartments Using Proton-killing Selection to Express Them at the Plasma Membrane

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Area of Science:

  • Cell biology
  • Ion channel physiology
  • Molecular mechanisms of cell volume regulation

Background:

  • Volume-regulated anion channels (VRAC) maintain cell volume during osmotic stress.
  • SWELL1 (LRRC8A) is a known essential VRAC component.
  • The pore-forming subunits and gating mechanisms of VRAC remain largely unknown.

Purpose of the Study:

  • To identify the pore-forming subunits of VRAC.
  • To elucidate the gating mechanism of VRAC by cell swelling.

Main Methods:

  • Biochemical reconstitution of LRRC8 complexes into lipid bilayers.
  • Electrophysiological recordings of reconstituted channels.
  • Analysis of channel activity under varying osmotic conditions and ionic strengths.

Main Results:

  • LRRC8 subunits (SWELL1 and others) assemble into heterogeneous VRAC complexes (~800 kDa).
  • Reconstituted LRRC8 complexes form functional anion channels activated by osmolality gradients.
  • Channel conductance is dependent on LRRC8 subunit composition.
  • Low cytoplasmic ionic strength activates LRRC8 complexes independently of osmotic gradients.

Conclusions:

  • LRRC8 proteins form the pore of the volume-regulated anion channel.
  • VRAC activation by hypotonic stress is mediated by a decrease in cytoplasmic ionic strength.