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Related Concept Videos

Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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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.
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Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
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Patch Clamp01:18

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Many fundamental cell functions such as muscle contraction and nerve transmission rely on the electrical signals produced by the movement of positively and negatively charged ions across the cell membrane. One competent method to record current flowing across the whole cell or single ion channel is the patch-clamp technique.
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Secondary Active Transport01:32

Secondary Active Transport

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One example of how cells use the energy contained in electrochemical gradients is demonstrated by glucose transport into cells. The ion vital to this process is sodium (Na+), which is typically present in higher concentrations extracellularly than in the cytosol. Such a concentration difference is due, in part, to the action of an enzyme "pump" embedded in the cellular membrane that actively expels Na+ from a cell. Importantly, as this pump contributes to the high concentration of...
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Updated: Jun 19, 2025

A Proteoliposome-Based Efflux Assay to Determine Single-molecule Properties of Cl- Channels and Transporters
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Insights into CLC-0's Slow-Gating from Intracellular Proton Inhibition.

Hwoi Chan Kwon1, Robert H Fairclough1,2, Tsung-Yu Chen1,2,3

  • 1Biophysics Graduate Program, University of California, Davis, CA 95618, USA.

International Journal of Molecular Sciences
|July 27, 2024
PubMed
Summary
This summary is machine-generated.

Intracellular protons (H+i) inhibit Torpedo CLC-0 channels by closing the slow gate, a process akin to inactivation. Anion flow through the pore speeds up slow-gate opening, revealing multiple inactivated states.

Keywords:
CLC channelCLC-0inactivationproton inhibitionslow gating

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Area of Science:

  • Molecular Biology
  • Ion Channel Physiology
  • Biophysics

Background:

  • The Torpedo CLC-0 chloride channel gating involves fast and slow mechanisms.
  • The slow gating mechanism's structural basis remains poorly understood.
  • Previous work linked intracellular proton (H+i) inhibition to slow-gate closure (inactivation).

Purpose of the Study:

  • To further elucidate the mechanism of H+i inhibition in wild-type CLC-0 and mutant channels.
  • To investigate the role of anion efflux in the recovery from H+i-induced inhibition.
  • To explore the nature of inactivated states in CLC-0 channels.

Main Methods:

  • Electrophysiological recordings of wild-type and mutant CLC-0 channels.
  • Application of intracellular protons (H+i) to induce channel inhibition.
  • Analysis of current recovery kinetics under various conditions, including anion efflux.
  • Utilizing inactivation-suppressed mutants to probe channel states.

Main Results:

  • Anion efflux through the CLC-0 pore accelerates recovery from H+i-induced inhibition, indicating slow-gate opening.
  • Inactivation-suppressed mutants display varied current recovery kinetics, suggesting multiple slow-gate closed (inactivated) states.
  • H+i likely increases anion binding affinity in the pore, initiating pore blockage and subsequent inactivation.

Conclusions:

  • H+i-induced inhibition of CLC-0 channels involves slow-gate closure, consistent with inactivation.
  • Anion permeation facilitates slow-gate opening, reversing H+i-induced inhibition.
  • The existence of multiple inactivated states is supported by differential recovery kinetics in mutants.