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...
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.
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.
Resting Potential Decay01:15

Resting Potential Decay

The resting membrane potential of a neuron (-70mV) is sustained due to the selective ion permeability of the membrane. At the resting potential, the membrane is slightly permeable to ions like sodium (Na+) and chloride (Cl−) and highly permeable to potassium ions (K+). Differences in the ions' concentration inside the cell compared to the outside are maintained by membrane transport proteins like channels and pumps.
At rest, the K+ is the main ion that moves across the membrane through...

You might also read

Related Articles

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

Sort by
Same author

Aging reveals divergent responses of AgRP/NPY neurons to diet in male and female mice.

bioRxiv : the preprint server for biology·2025
Same author

The Missing Half: Why Sex Differences Matter in Alzheimer's Disease.

Biological psychiatry·2025
Same author

The Shab family potassium channels are highly enriched at the presynaptic terminals of human neurons.

The Journal of biological chemistry·2025
Same author

Detecting the effect of genetic diversity on brain composition in an Alzheimer's disease mouse model.

Communications biology·2024
Same author

An in vitro neurogenetics platform for precision disease modeling in the mouse.

Science advances·2024
Same author

New directions for Alzheimer's disease research from the Jackson Laboratory Center for Alzheimer's and Dementia Research 2022 workshop.

Alzheimer's & dementia (New York, N. Y.)·2024

Related Experiment Video

Updated: Jun 12, 2026

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique
08:11

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

Localization-dependent activity of the Kv2.1 delayed-rectifier K+ channel.

Kristen M S O'Connell1, Robert Loftus, Michael M Tamkun

  • 1Department of Biomedical Sciences, Colorado State University, Fort Collins, CO 80523, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 23, 2010
PubMed
Summary

Kv2.1 potassium channels cluster on neuronal surfaces, but these clusters do not conduct ions. Non-clustered Kv2.1 channels are responsible for neuronal excitability regulation.

More Related Videos

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

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

Related Experiment Videos

Last Updated: Jun 12, 2026

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique
08:11

Voltage-Dependent Potassium Current Recording on H9c2 Cardiomyocytes via the Whole-Cell Patch-Clamp Technique

Published on: November 11, 2022

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting
10:08

Study of the Functions and Activities of Neuronal K-Cl Co-Transporter KCC2 Using Western Blotting

Published on: December 9, 2022

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

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biophysics

Background:

  • Kv2.1 potassium channels are crucial for regulating neuronal excitability, particularly during high-frequency stimulation.
  • These channels uniquely form large clusters on neuronal soma and dendrites, a phenomenon also observed in transfected HEK cells.

Purpose of the Study:

  • To investigate the functional role of Kv2.1 channel localization and clustering on neuronal surfaces.
  • To determine if clustered and non-clustered Kv2.1 channels exhibit different conductive properties and voltage sensitivities.

Main Methods:

  • Utilized cell-attached patch clamp technique to assess Kv2.1 channel activity at different cellular locations.
  • Investigated the effects of actin depolymerization and alkaline phosphatase treatment on Kv2.1 channel clustering and function.

Main Results:

  • Clustered Kv2.1 channels showed inefficient potassium ion (K+) conductance, while non-clustered channels mediated the typical high-threshold delayed rectifier K+ current.
  • Only approximately 2% of surface Kv2.1 channels were found to conduct ions, indicating that clustered channels remain responsive to membrane potential changes.
  • Declustering induced by actin depolymerization or dephosphorylation did not enhance whole-cell currents, suggesting clusters are not a reservoir of non-conducting channels.

Conclusions:

  • Kv2.1 clusters do not house high-threshold channels whose voltage sensitivity changes upon declustering.
  • Kv2.1 clusters are not a reservoir of silent channels activated upon release.
  • Proposed unique, non-conductive roles for clustered Kv2.1 channels, independent of K+ conductance.