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...
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...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that include the...
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.

You might also read

Related Articles

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

Sort by
Same author

Autonomic nervous system dysregulation as a driver of atrial fibrillation: pathways, modulators, and therapies.

American journal of physiology. Cell physiology·2026
Same author

A novel nomogram based on HALP score for predicting time to glycemic stability in hospitalized type 2 diabetes patients.

Frontiers in endocrinology·2026
Same author

Predicting time to glycemic stability in hospitalized type 2 diabetes patients using insulin resistance indices: a nomogram development and validation study.

Endocrine connections·2026
Same author

Wearable Cardiac Devices as Windows Into Physiological Decline: A Review of Digital Biomarkers in the Prevention, Detection, and Management of Cardiogeriatric Frailty.

Heart, lung & circulation·2026
Same author

Cardiac resynchronization therapy with or without atrioventricular node ablation in atrial fibrillation: the CAAN-AF trial.

European heart journal·2026
Same author

Building Australia's non-animal technologies ecosystem: a national cross-sector mapping and strategic insights from the non-animal technologies network (NAT-Net).

Frontiers in toxicology·2026

Related Experiment Video

Updated: May 18, 2026

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

hERG K(+) channels: structure, function, and clinical significance.

Jamie I Vandenberg1, Matthew D Perry, Mark J Perrin

  • 1Mark Cowley Lidwill Research Programme in Cardiac Electrophysiology, Victor Chang Cardiac Research Institute, Sydney, New South Wales, Australia. j.vandenberg@victorchang.edu.au

Physiological Reviews
|September 20, 2012
PubMed
Summary

The human ether-a-go-go related gene (hERG) encodes Kv11.1 channels, crucial for heart function. Dysfunction causes long QT syndrome and drug-induced arrhythmias, highlighting their critical role in cardiac health.

More Related Videos

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

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry
11:32

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry

Published on: September 28, 2016

Related Experiment Videos

Last Updated: May 18, 2026

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

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

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry
11:32

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry

Published on: September 28, 2016

Area of Science:

  • Cardiovascular Physiology
  • Molecular Biology
  • Pharmacology

Background:

  • The human ether-a-go-go related gene (hERG) encodes the Kv11.1 channel, a key component of cardiac electrical activity.
  • Kv11.1 channels are implicated in long QT syndrome (LQTS) and drug-induced QT prolongation, both linked to life-threatening arrhythmias.
  • While expressed in various tissues, their cardiac role is most extensively studied due to clinical significance.

Purpose of the Study:

  • To review the biogenesis, trafficking, gating, and pharmacology of Kv11.1 channels.
  • To explore the pathophysiology of Kv11.1 channel dysfunction in cardiac disorders.
  • To consolidate current knowledge on hERG channel function and clinical relevance.

Main Methods:

  • Literature review of studies on hERG channel properties.
  • Analysis of genetic and pharmacological data related to Kv11.1 channels.
  • Synthesis of information on Kv11.1 channel's role in cardiac electrophysiology and disease.

Main Results:

  • Detailed discussion of Kv11.1 channel biogenesis, membrane trafficking, and gating mechanisms.
  • Overview of Kv11.1 channel pharmacology, including drug interactions and blockade.
  • Elucidation of the molecular basis for LQTS and drug-induced QT prolongation linked to hERG.

Conclusions:

  • Kv11.1 channels are critical determinants of cardiac repolarization and are central to understanding LQTS and drug-induced arrhythmias.
  • Understanding hERG channel properties and pathophysiology is essential for preventing sudden cardiac death.
  • Further research into Kv11.1 channel function may lead to improved therapeutic strategies for cardiac channelopathies.