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

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

6.4K
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...
6.4K
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

12.4K
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...
12.4K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

2.3K
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...
2.3K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

8.3K
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...
8.3K
Non-gated Ion Channels01:24

Non-gated Ion Channels

6.9K
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....
6.9K
The Role of Ion Channels in Neuronal Computation01:19

The Role of Ion Channels in Neuronal Computation

3.2K
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....
3.2K

You might also read

Related Articles

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

Sort by
Same author

Structural basis for activation and potentiation in a human α5β3 GABA<sub>A</sub> receptor.

Nature communications·2026
Same author

Lipid bilayers determine allostery but not intrinsic affinity of cAMP to pacemaker channels.

Nature communications·2026
Same author

Mechanistic insights into the therapeutic properties of delta opioid receptor.

Science advances·2026
Same author

Caveolar Compartmentalization of Pacemaker Signaling Ensures Stable Sinoatrial Rhythmicity Which Is Disrupted in Heart Failure.

JACC. Clinical electrophysiology·2026
Same author

Ligand Binding Dynamics of Ion Channels and GPCRs Using Single-Molecule Fluorescence.

Annual review of biophysics·2026
Same author

A critical residue mediates proper assembly and gating of GIRK2 channels.

The Journal of general physiology·2025

Related Experiment Video

Updated: Jul 17, 2025

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

13.6K

Structural Basis for Hyperpolarization-dependent Opening of the Human HCN1 Channel.

Verena Burtscher1,2,3, Jonathan Mount4,2,5,3, John Cowgill1,2,6

  • 1Department of Anesthesiology, Washington University School of Medicine, Saint Louis, MO, USA.

Biorxiv : the Preprint Server for Biology
|August 30, 2023
PubMed
Summary

Hyperpolarization and cyclic-nucleotide (HCN) activated ion channels control heart rhythm. Cryo-EM structures reveal how gating charges move to open these crucial HCN channels.

More Related Videos

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b
10:20

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b

Published on: November 11, 2016

8.6K
One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

24.4K

Related Experiment Videos

Last Updated: Jul 17, 2025

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

13.6K
Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b
10:20

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b

Published on: November 11, 2016

8.6K
One-channel Cell-attached Patch-clamp Recording
13:07

One-channel Cell-attached Patch-clamp Recording

Published on: June 9, 2014

24.4K

Area of Science:

  • Structural Biology
  • Ion Channel Physiology

Background:

  • Hyperpolarization and cyclic-nucleotide (HCN) activated ion channels are vital for pacemaking and rhythmic electrical activity.
  • Unlike typical voltage-gated channels, HCN channels open upon hyperpolarization, a mechanism not fully understood structurally.

Approach:

  • Cryo-electron microscopy (cryo-EM) was used to determine the structures of human HCN1 channels in Closed, Intermediate, and Open states.
  • Analysis focused on the movement of gating charges and conformational changes in transmembrane helices (S4, S5, S6) during channel gating.

Key Points:

  • Inward movement of gating charges past the charge transfer center (CTC) and S5 helix tilting drive pore opening.
  • The Intermediate state shows one gating charge below CTC with a closed pore; the Open state has both charges past CTC and a fully open pore.
  • Voltage sensor motion causes unwinding of S4/S5 helices, disrupting the closed-state interface and leading to iris-like S5/S6 displacement and pore opening.

Conclusions:

  • The study reveals the structural basis for HCN channel gating, involving charge movement and helix unwinding.
  • These findings elucidate the unique reversed voltage-dependence of HCN channels.