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...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

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...
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...
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

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

Science advances·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

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

Nature·2025
Same author

Activation of the Voltage-Gated Potassium Channel by Amphiphilic Glycopeptides.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Peptide toxins as tools in ion channel biology.

Current opinion in chemical biology·2025
Same author

Conservation of the cooling agent binding pocket within the TRPM subfamily.

eLife·2024
Same journal

Application of ephrin-B2 loaded glycol chitosan-silk fibroin hydrogel in the treatment of diabetic refractory wounds.

Scientific reports·2026
Same journal

International expert Delphi consensus on thromboprophylaxis in metabolic and bariatric surgery.

Scientific reports·2026
Same journal

Assessing the cross-region knowledge transfer capability of selected deep learning building vectorization methods in the context of available training datasets.

Scientific reports·2026
Same journal

Feasibility and preliminary effects of outdoor versus indoor cognitive-motor therapy in women with Alzheimer's disease: A randomized single-blind pilot study.

Scientific reports·2026
Same journal

Hallmarks of social action in the vocal turn-taking of wild common marmosets (Callithrix jacchus).

Scientific reports·2026
Same journal

Role and mechanism of AOPPs-induced NOX4-mediated ferroptosis in intervertebral disc degeneration.

Scientific reports·2026
See all related articles

Related Experiment Video

Updated: May 13, 2026

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

Exploring structure-function relationships between TRP and Kv channels.

Jeet Kalia1, Kenton J Swartz

  • 1Porter Neuroscience Research Center, Molecular Physiology and Biophysics Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health 35 Convent Drive, Bethesda, Maryland 20892, USA.

Scientific Reports
|March 23, 2013
PubMed
Summary
This summary is machine-generated.

Investigating ion channel structure-function, this study found that the S3b-S4 paddle motif of voltage-activated potassium (Kv) channels can be replaced by similar regions from Transient Receptor Potential (TRP) channels, but not vice versa.

More Related Videos

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Related Experiment Videos

Last Updated: May 13, 2026

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

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability

Published on: June 2, 2023

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

Area of Science:

  • Molecular Biology
  • Ion Channel Physiology
  • Structural Biology

Background:

  • The activation mechanisms of Transient Receptor Potential (TRP) ion channels are less understood than those of voltage-activated potassium (Kv) channels.
  • Structural and pharmacological similarities between TRP and Kv channels suggest potential commonalities in their structure-function relationships.

Purpose of the Study:

  • To test the hypothesis that Kv and TRP ion channels share common structure-function features.
  • To investigate the functional impact of interchanging specific domains between Kv2.1 and TRP channels (TRPM8, TRPV1).

Main Methods:

  • Utilized domain-swapping experiments, replacing membrane-spanning regions of Kv2.1 with corresponding motifs from TRPM8 and TRPV1.
  • Assessed the functional consequences of these chimeric constructs on channel voltage-activation properties.

Main Results:

  • The S3b-S4 paddle motif of Kv2.1 could be successfully replaced by analogous regions from TRPM8 and TRPV1, preserving voltage-activation.
  • Conversely, attempts to replace TRP channel domains with Kv2.1 regions resulted in non-functional channels.
  • These findings indicate limited structural compatibility for creating functional hybrid channels between these two families.

Conclusions:

  • The S3b-S4 paddle motif represents a conserved functional element or a region tolerant to substitution between Kv and TRP channels.
  • Significant structural divergence exists between most domains of TRP and Kv channels, hindering the formation of functional hybrids.
  • This study highlights specific structural differences that contribute to the distinct activation mechanisms of these major ion channel families.