Jove
Visualize
Contact Us

Related Concept Videos

Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

8.2K
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...
8.2K
Destabilization of Microtubules01:45

Destabilization of Microtubules

2.7K
The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
2.7K
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

You might also read

Related Articles

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

Sort by
Same author

Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.

Science advances·2026
Same author

On the effect of lateral stretch on the deformation energetics of biological membranes and the lipid dynamics within.

bioRxiv : the preprint server for biology·2026
Same author

Distinct mechanisms of inhibition of Kv2 potassium channels by tetraethylammonium and RY785.

eLife·2026
Same author

Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.

bioRxiv : the preprint server for biology·2025
Same author

Molecular basis for the regulation of membrane proteins through preferential lipid solvation.

Nature chemical biology·2025
Same author

Structural basis of fast N-type inactivation in K<sub>v</sub> channels.

Nature·2025
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 Experiment Video

Updated: Jul 9, 2025

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

19.4K

Eukaryotic Kv channel Shaker inactivates through selectivity filter dilation rather than collapse.

Robyn Stix1,2, Xiao-Feng Tan3, Chanhyung Bae3

  • 1Theoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Science Advances
|December 8, 2023
PubMed
Summary

Structural studies reveal that eukaryotic voltage-gated potassium channels undergo C-type inactivation by dilating their selectivity filter. This atomic-level insight explains channel function and regulation.

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

19.1K
Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

13.4K

Related Experiment Videos

Last Updated: Jul 9, 2025

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

19.4K
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

19.1K
Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes
11:33

Isolation and Kv Channel Recordings in Murine Atrial and Ventricular Cardiomyocytes

Published on: March 12, 2013

13.4K

Area of Science:

  • Molecular biology
  • Structural biology
  • Biophysics

Background:

  • Eukaryotic voltage-gated K+ channels are crucial for neuronal signaling.
  • C-type inactivation is a key regulatory mechanism, but its structural basis is unclear.

Purpose of the Study:

  • To determine the atomic structure of wild-type K+ channels in the C-type inactivated state.
  • To elucidate the molecular mechanism underlying K+ channel C-type inactivation.

Main Methods:

  • Atomic-resolution cryo-electron microscopy (cryo-EM) of wild-type Shaker K+ channels.
  • All-atom molecular dynamics simulations.

Main Results:

  • Cryo-EM revealed a dilated selectivity filter in the wild-type channel, consistent with C-type inactivation.
  • Simulations confirmed this conformation explains residual ion conductance and altered ion selectivity.
  • Simulations also rationalized the effects of mutations on inactivation rates.

Conclusions:

  • The study establishes the molecular basis of C-type inactivation in eukaryotic K+ channels.
  • The dilated selectivity filter is the structural hallmark of this auto-inhibitory mechanism.
  • This provides a foundation for understanding K+ channel regulation and dysfunction.