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Related Concept Videos

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...
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...
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

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.
Sometimes a single EPSP is strong enough to induce an action potential in the postsynaptic neuron. However, multiple presynaptic inputs must often create EPSPs around the same time for the postsynaptic neuron to be sufficiently depolarized to fire an action potential.
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
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...

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Related Experiment Video

Updated: May 10, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

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

Published on: December 9, 2022

Ca2+-activated Cl- channels.

Loretta Ferrera1, Olga Zegarra-Moran, Luis J V Galietta

  • 1Laboratory of Molecular Genetics, Istituto Giannina Gaslini, Genova, Italy.

Comprehensive Physiology
|June 5, 2013
PubMed
Summary

Calcium-activated chloride channels (CaCCs), identified as TMEM16A and TMEM16B, are crucial for physiological processes. Their dysfunction impacts Cl(-) secretion and gastrointestinal motility.

Area of Science:

  • Physiology
  • Molecular Biology
  • Ion Channels

Background:

  • Calcium-activated chloride channels (CaCCs) are vital plasma membrane proteins.
  • CaCCs regulate anion secretion in epithelial cells and influence electrical activity in smooth muscle and nervous system cells.

Purpose of the Study:

  • To identify the molecular components responsible for CaCC activity.
  • To investigate the physiological roles of TMEM16A and TMEM16B in Cl(-) transport and cellular function.

Main Methods:

  • Transfection of TMEM16A and TMEM16B into null cells to assess CaCC currents.
  • RNA interference (RNAi) to silence TMEM16A expression.
  • Analysis of TMEM16A-deficient mice to evaluate physiological consequences.

Main Results:

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One-channel Cell-attached Patch-clamp Recording
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One-channel Cell-attached Patch-clamp Recording

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Related Experiment Videos

Last Updated: May 10, 2026

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

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

Published on: December 9, 2022

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

  • Expression of TMEM16A and TMEM16B in null cells reconstituted Ca(2+)-activated Cl(-) currents.
  • Silencing TMEM16A abolished CaCC activity in various cell types, including airway epithelium and smooth muscle.
  • TMEM16A-deficient mice exhibited impaired Cl(-) secretion and loss of gastrointestinal motility.

Conclusions:

  • TMEM16A and TMEM16B are confirmed as CaCC-forming proteins.
  • TMEM16A plays a critical role in epithelial anion secretion and gastrointestinal function.
  • Understanding TMEM16 proteins is key to elucidating the molecular basis of chloride transport.