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

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.
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.
Gap Junctions01:27

Gap Junctions

The cytoplasm of adjacent animal cells can exchange small molecules, ions, and secondary messengers via the communication channels which form the gap junctions. These junctions comprise a few hundred to thousands of molecular channels, each made of two halves, called the connexon hemichannel. A connexon is a hexamer of six transmembrane connexin proteins, which assemble radially, thus forming a pore or channel in the center. One connexon hemichannel docks with a corresponding connexon on the...

You might also read

Related Articles

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

Sort by
Same author

The perijunctional zone is a molecularly distinct muscle subdomain altered in Duchenne muscular dystrophy.

Nature communications·2026
Same author

AXIS of excitability: microglia promote neuronal firing.

Cell research·2026
Same author

Diverse and location-specific roles of PlexinA2, PlexinA4, and NCAM in developing hippocampal mossy fibers.

Translational psychiatry·2026
Same author

A distinct PP2A subunit regulates local protein phosphorylation at the axon initial segment.

Nature communications·2025
Same author

OASIS: in vivo AAV-mediated transduction and genome editing of adult oligodendrocytes.

bioRxiv : the preprint server for biology·2025
Same author

Muscle spectrin.

The Journal of physiology·2025
Same journal

Dynorphinergic neuroadaptations in the islands of Calleja: implications for alcohol use disorder.

Neuroscience letters·2026
Same journal

Differential vulnerability of cochlear nuclei to Lmx1 deficiency: abnormal patterning and implications for auditory circuitry.

Neuroscience letters·2026
Same journal

Role of nNOS/sGC pathway in the insular cortex in control of cardiovascular, autonomic and corticosterone responses to restraint stress in rats.

Neuroscience letters·2026
Same journal

Jak1 inhibition reduces acute allodynia induced by specific upstream cytokines in rats: implications for the onset of Jak1 pain modulation.

Neuroscience letters·2026
Same journal

Glucocorticoids-induced depressive-like behaviors in mice: oral ingestion of corticosterone or hydrocortisone - A comparative study.

Neuroscience letters·2026
Same journal

Data-driven clustering of prefrontal activation identifies functional phenotypes under prioritized dual-task walking conditions in Parkinson's disease.

Neuroscience letters·2026
See all related articles

Related Experiment Video

Updated: Jun 9, 2026

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

Clustered K+ channel complexes in axons.

Matthew N Rasband1

  • 1Department of Neuroscience, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, United States. Rasband@bcm.edu

Neuroscience Letters
|September 7, 2010
PubMed
Summary
This summary is machine-generated.

Voltage-gated potassium (Kv) channels are crucial for neuronal function. This review explores how protein complexes recruit these essential Kv channels to specific locations within axons.

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

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

Related Experiment Videos

Last Updated: Jun 9, 2026

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes
10:19

Patch Clamp and Perfusion Techniques for Studying Ion Channels Expressed in Xenopus oocytes

Published on: January 10, 2011

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

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

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Voltage-gated potassium (Kv) channels are critical regulators of neuronal electrical activity, influencing action potential dynamics and neurotransmitter release.
  • These channels are precisely localized to specific domains within neuronal axons, such as the axon initial segment and nodes of Ranvier.
  • The precise localization of Kv channels is essential for their proper function in neuronal signaling.

Purpose of the Study:

  • To review the composition and function of protein complexes that localize Kv channels in axons.
  • To elucidate the mechanisms by which these complexes recruit Kv channels to distinct axonal domains.
  • To highlight the importance of these complexes in regulating neuronal properties.

Main Methods:

  • Literature review of studies on Kv channel localization in axons.
  • Analysis of molecular composition of Kv channel complexes.
  • Examination of functional roles of interacting proteins in Kv channel targeting.

Main Results:

  • Kv channels form large complexes with cell adhesion molecules and scaffolding proteins.
  • These interacting proteins are key determinants for recruiting Kv channels to specific axonal sites.
  • Complex composition varies depending on the axonal domain.

Conclusions:

  • Protein complexes play a vital role in the targeted localization of Kv channels in axons.
  • Understanding these complexes provides insights into the regulation of neuronal excitability.
  • Further research into these complexes could reveal novel therapeutic targets for neurological disorders.