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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...
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...
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.
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...

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Updated: May 21, 2026

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

Structural determinants at KCNE4 position 145 govern Kv1.3 channel function.

Magalí Colomer-Molera1, Daniel Sastre1, Antonio Felipe1

  • 1Molecular Physiology Laboratory, Departament de Bioquímica i Biomedicina Molecular, Institut de Biomedicina (IBUB), Universitat de Barcelona, Barcelona, Spain.

The Journal of General Physiology
|May 20, 2026
PubMed
Summary
This summary is machine-generated.

The KCNE4 protein regulates Kv1.3 channels involved in immune cell function. Specific KCNE4 variants impact Kv1.3 channel activity, potentially influencing immune system disorders.

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Last Updated: May 21, 2026

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Published on: March 12, 2013

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biophysics

Background:

  • Potassium voltage-gated channel subfamily A member 3 (Kv1.3) channels are crucial for leukocyte activation and proliferation.
  • The KCNE4 regulatory subunit negatively modulates Kv1.3 channel function.
  • KCNE4 interacts with Kv1.3, affecting its trafficking, current density, and inactivation kinetics.

Purpose of the Study:

  • To investigate the functional impact of KCNE4 variants on Kv1.3 channel activity.
  • To explore the role of specific amino acid residues within the KCNE4 protein in regulating Kv1.3.
  • To understand the structural determinants of KCNE4's regulatory function on Kv1.3.

Main Methods:

  • Site-directed mutagenesis to create KCNE4 variants.
  • Electrophysiological recordings (e.g., two-electrode voltage clamp) to measure Kv1.3 currents.
  • Confocal microscopy to assess Kv1.3 channel trafficking to the plasma membrane.

Main Results:

  • Both investigated KCNE4 variants impaired forward trafficking of Kv1.3 channels to the plasma membrane.
  • A variant-dependent decrease in Kv1.3 macroscopic currents was observed, with minimal effects on channel kinetics.
  • The charge and size of the central amino acid within an anionic triplet (D-D/E-E) of KCNE4 are critical for modulating Kv1.3 currents.

Conclusions:

  • KCNE4 variants can alter Kv1.3 channel function by affecting trafficking and current magnitude.
  • The central residue of the anionic cluster in KCNE4 plays a key role in regulating Kv1.3 channel activity.
  • Understanding these interactions may provide insights into immune system disorders linked to Kv1.3 and KCNE4.