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Related Concept Videos

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.
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...
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...
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.
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...
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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Related Experiment Video

Updated: Jun 21, 2026

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 11, 2011

Modulation of Kv4.3 current by accessory subunits.

Isabelle Deschênes1, Gordon F Tomaselli

  • 1Department of Medicine, Institute of Molecular Cardiobiology, Division of Cardiology, Johns Hopkins University, Baltimore, MD 21205, USA.

FEBS Letters
|September 26, 2002
PubMed
Summary

Cardiac potassium channel Kv4.3 interacts with multiple accessory subunits. These interactions significantly alter Kv4.3 current properties, though their precise physiological roles remain unclear.

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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

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Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
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Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

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Related Experiment Videos

Last Updated: Jun 21, 2026

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 11, 2011

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
11:42

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

Published on: January 22, 2015

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

Area of Science:

  • Molecular biology
  • Cardiovascular physiology
  • Ion channel function

Background:

  • Kv4.3 is the main pore-forming subunit of cardiac transient outward potassium current (I(to)).
  • Native cardiac I(to) is not fully replicated by hKv4.3 alone, indicating the involvement of accessory subunits.
  • KChIP2, a known Kv4.3-interacting protein, modifies currents but doesn't fully replicate native I(to).

Purpose of the Study:

  • To investigate the impact of various cardiac ancillary subunits on hKv4.3-encoded currents.
  • To determine if ancillary subunits can modulate the biophysical properties of hKv4.3 currents.

Main Methods:

  • Co-expression of hKv4.3 with different ancillary subunits (Kvbeta(3), minK, MiRP-1, Na channel beta(1), KChIP2) in a heterologous expression system.
  • Electrophysiological recordings to analyze current density and gating kinetics.

Main Results:

  • Several ancillary subunits, including Kvbeta(3), minK, MiRP-1, Na channel beta(1), and KChIP2, significantly increased the density of hKv4.3 currents.
  • These ancillary subunits also modified the voltage-dependence and kinetics of hKv4.3 channel gating.
  • hKv4.3 demonstrated promiscuous assembly with multiple ancillary subunits in vitro.

Conclusions:

  • hKv4.3 exhibits broad assembly capabilities with various ancillary subunits.
  • These interactions lead to significant functional modifications of hKv4.3 currents.
  • The precise physiological relevance of these promiscuous interactions in native cardiac I(to) requires further investigation.