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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.
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.
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...

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Related Experiment Video

Updated: Jul 23, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

Structural conservation in prokaryotic and eukaryotic potassium channels

R MacKinnon1, S L Cohen, A Kuo

  • 1Laboratory of Molecular Neurobiology and Biophysics and the Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. mackinn@rockvax.rockefeller.edu

Science (New York, N.Y.)
|April 29, 1998
PubMed
Summary

Scorpion venom toxins were screened against bacterial potassium channels (K+ channels). Researchers found that prokaryotic K+ channels share structural similarities with eukaryotic ones, opening new avenues for K+ channel drug discovery.

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Recapitulation of an Ion Channel IV Curve Using Frequency Components

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Last Updated: Jul 23, 2026

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells
15:28

Mutagenesis and Functional Analysis of Ion Channels Heterologously Expressed in Mammalian Cells

Published on: October 1, 2010

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

Recapitulation of an Ion Channel IV Curve Using Frequency Components
10:14

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Potassium channels (K+ channels) are crucial transmembrane proteins involved in numerous physiological processes.
  • Scorpion venoms contain diverse toxins that often target ion channels, including K+ channels.
  • Understanding K+ channel structure and function is vital for developing therapeutic agents.

Purpose of the Study:

  • To screen scorpion venom for toxins that interact with potassium channels.
  • To investigate the structural conservation between prokaryotic and eukaryotic K+ channels.
  • To establish a novel approach for K+ channel pharmacology.

Main Methods:

  • Utilized resin-attached, mutant K+ channels from Streptomyces lividans for high-throughput screening.
  • Employed mass spectrometry for rapid identification of venom toxins interacting with K+ channels.
  • Conducted mutagenesis and radioligand binding assays to characterize specific toxin-channel interactions.

Main Results:

  • Successfully screened venom from Leiurus quinquestriatus hebraeus against bacterial K+ channels.
  • Identified specific toxins, including agitoxin2, that bind to the K+ channel.
  • Demonstrated that a prokaryotic K+ channel possesses a pore structure conserved with eukaryotic K+ channels.

Conclusions:

  • Prokaryotic K+ channels serve as valuable models for studying eukaryotic K+ channel structure.
  • The developed screening and characterization techniques offer a new platform for K+ channel drug discovery.
  • Structural conservation highlights potential for broad applications in K+ channel pharmacology.