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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.
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 Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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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Related Experiment Video

Updated: May 21, 2026

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique
08:11

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

Voltage sensor inactivation in potassium channels.

Robert Bähring1, Jan Barghaan, Regina Westermeier

  • 1Institut für Zelluläre und Integrative Physiologie, Zentrum für Experimentelle Medizin, Universitätsklinikum Hamburg-Eppendorf Hamburg, Germany.

Frontiers in Pharmacology
|June 2, 2012
PubMed
Summary

Voltage-gated potassium channel inactivation occurs via two distinct mechanisms: P/C-type inactivation, involving the pore gate, and A/C-type inactivation, involving the activation gate. These represent two forms of voltage sensor inactivation.

Keywords:
Kv channelsP/C-type inactivationU-type inactivationclosed-state inactivation

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Area of Science:

  • Molecular and Cellular Neuroscience
  • Ion Channel Physiology
  • Biophysics

Background:

  • Voltage-gated potassium (Kv) channels control cellular excitability through voltage-dependent gating.
  • Depolarization triggers voltage sensor domain movement, leading to pore opening.
  • Kv channel function is modulated by inactivation mechanisms, impacting cellular signaling.

Purpose of the Study:

  • To elucidate the distinct mechanisms underlying Kv channel inactivation.
  • To differentiate between pore gate (P/C-type) and activation gate (A/C-type) involvement in inactivation.
  • To introduce and define 'A/C-type inactivation' as a novel form of voltage sensor inactivation.

Main Methods:

  • Analysis of voltage sensor domain movement and its interaction with pore domain gates.
  • Investigating conformational changes in the S6 bundle crossing (A-gate) and selectivity filter (P-gate).
  • Characterizing inactivation modes based on voltage sensor coupling with activation and pore gates.

Main Results:

  • Kv channel inactivation is determined by the voltage sensor's interaction with either the P-gate or the A-gate.
  • P/C-type inactivation involves tight interaction with the P-gate, leading to selectivity filter non-conductivity.
  • A/C-type inactivation involves temporary uncoupling from the A-gate, favoring inactivation from pre-open closed states.

Conclusions:

  • Kv channel inactivation comprises two mechanistically distinct pathways: P/C-type and A/C-type inactivation.
  • Both P/C-type and A/C-type inactivation are forms of 'voltage sensor inactivation'.
  • Understanding these inactivation modes is crucial for comprehending Kv channel function and regulation.