Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

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...
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.
Ion Channels01:19

Ion Channels

The movement of ions like sodium, potassium, and calcium into and out of the cell is essential to maintain the electrochemical gradient in living cells. The ion channels—a class of membrane transport proteins—help maintain this ionic gradient for the smooth functioning of physiological activities such as maintaining cell size and volume, conducting nerve impulses, and gas and nutrient exchange.
Ion channels are specialized integral membrane proteins on the plasma membrane that allow specific...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Cognitive Decline, Neurologic Involvement, and Neonatal Crisis in <i>ABCC9</i>-Related Intellectual Disability and Myopathy Syndrome.

Neurology. Genetics·2026
Same author

Functional screen for subtype specificity of voltage sensor-targeted Kv7 potentiators.

British journal of pharmacology·2026
Same author

Subunit composition of the KATP channels that modulate contractility of skeletal muscle during fatigue.

The Journal of general physiology·2026
Same author

Natural xanthones as α-Mangostin induce vasorelaxation involving key gating residues in the S6 domain of BK channels.

eLife·2026
Same author

Localized phosphoinositide metabolism regulates STIM1/ORAI1 fast inactivation.

iScience·2026
Same author

Proton channels govern vesicular carbonate chemistry in mineralizing cells of a marine calcifier.

Nature communications·2026
Same journal

Sequential neural dynamics underlie unconscious integration and conscious perception of visual stimuli.

PLoS biology·2026
Same journal

Engineering resilient gene drives for sustainable malaria control by predicting, testing and overcoming target site resistance in Anopheles gambiae.

PLoS biology·2026
Same journal

Shared memories of event details in the human brain are altered by misinformation and test expectations.

PLoS biology·2026
Same journal

Resistance potentiators: Evolutionary catalysts of antibiotic resistance.

PLoS biology·2026
Same journal

The cell cloud: Adopting systems biology concepts in the era of single-cell immunology.

PLoS biology·2026
Same journal

Disinhibitory signaling enables flexible coding of top-down information in cortical networks.

PLoS biology·2026
See all related articles

Related Experiment Video

Updated: Jun 15, 2026

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

Voltage-dependent gating in a "voltage sensor-less" ion channel.

Harley T Kurata1, Markus Rapedius, Marc J Kleinman

  • 1Department of Anesthesiology, Pharmacology, and Therapeutics, University of British Columbia, Vancouver, Canada. hkurata@interchange.ubc.ca

Plos Biology
|March 9, 2010
PubMed
Summary
This summary is machine-generated.

A mutation in the ligand-gated Kir6.2 channel confers voltage dependence, revealing new insights into ion channel gating mechanisms. This finding suggests inherent voltage sensitivity in channels previously thought to be ligand-gated only.

More Related Videos

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

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

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

Related Experiment Videos

Last Updated: Jun 15, 2026

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

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

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

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

Area of Science:

  • Molecular Biology
  • Biophysics
  • Ion Channel Physiology

Background:

  • Voltage-gated cation channels typically rely on dedicated voltage-sensing domains for function.
  • Kir6.2 channels are primarily known as ligand-gated potassium channels, lacking canonical voltage-sensing domains.

Purpose of the Study:

  • To investigate the voltage dependence of the Kir6.2 channel.
  • To explore the interaction between ligand-gating and voltage-dependent gating mechanisms in ion channels.

Main Methods:

  • Site-directed mutagenesis to create the Kir6.2[L157E] mutant.
  • Electrophysiological recordings to analyze channel gating properties.
  • Manipulation of intracellular and membrane lipid compositions (PIP2) to assess gating modulation.

Main Results:

  • A point mutation (L157E) introduced voltage dependence to the Kir6.2 channel.
  • The Kir6.2[L157E] mutant displayed time-dependent activation upon depolarization, similar to Kv channels.
  • Voltage dependence was modulated by PIP2 levels and ATP, interacting with ligand-gating mechanisms.
  • Gating of the mutant channel showed sensitivity to intracellular potassium concentration, linking permeation and gating.

Conclusions:

  • Demonstrates inherent voltage dependence in a ligand-gated K+ channel, challenging existing paradigms.
  • Provides a framework for understanding the interplay between ion permeation and gating.
  • Suggests that voltage-dependent gating may be a latent feature across the cation channel superfamily.