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

Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

4.8K
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...
4.8K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

8.1K
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...
8.1K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

4.6K
4.6K
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

6.9K
GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
6.9K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

13.1K
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...
13.1K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

6.4K
6.4K

You might also read

Related Articles

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

Sort by
Same author

Glycolipids slow interfacial proton migration while preserving surface proton retention.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Calculation of Green Function for the Problem of Mechanical Indentation of Supported Lipid Bilayer.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Optical control of carrier-mediated ion transport by photoswitchable lipids.

Nanoscale·2025
Same author

Molecular Interactions within Nanoconfinement of Model DNA Nanostructures Controlled by Compensatory Kinetics as Revealed by Single-Molecule Fluorescence Analysis.

JACS Au·2025
Same author

Adsorption of Bovine Serum Albumin to Lipid Membranes Increases the Number and Stability of Ion Channels of Gramicidin A.

Langmuir : the ACS journal of surfaces and colloids·2025
Same author

Clear Native Gel Electrophoresis for the Purification of Fluorescently Labeled Membrane Proteins in Native Nanodiscs.

Analytical chemistry·2025

Related Experiment Video

Updated: Mar 31, 2026

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

20.1K

Modulation of Kv Channel Gating by Light-Controlled Membrane Thickness.

Rohit Yadav1, Juergen Pfeffermann1, Nikolaus Goessweiner-Mohr1

  • 1Institute of Biophysics, Johannes Kepler University Linz, 4040 Linz, Austria.

Biomolecules
|May 28, 2025
PubMed
Summary
This summary is machine-generated.

Membrane thickness directly controls voltage-gated potassium (Kv) channel activity. Light-induced membrane changes reversibly modulated KvAP channel function, demonstrating a link between membrane mechanics and voltage sensing.

Keywords:
Kv channelelectrophysiologyphotoswitchable lipidsvoltage sensor

More Related Videos

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

20.1K
Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

2.4K

Related Experiment Videos

Last Updated: Mar 31, 2026

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

20.1K
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

20.1K
Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

2.4K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Membrane Protein Dynamics

Background:

  • Voltage-gated potassium (Kv) channels are crucial for neuronal electrical activity.
  • Anionic lipids are known to influence Kv channel gating, but the precise mechanisms are unclear.
  • Previous studies suggested a link between membrane thinning and Kv channel down states.

Purpose of the Study:

  • To investigate the direct impact of membrane thickness on voltage-gated potassium channel function.
  • To explore a novel, light-controlled method for modulating ion channel activity.
  • To establish a mechanistic link between membrane mechanics and voltage-sensing domains.

Main Methods:

  • Reconstitution of Aeropyrum pernix Kv channels (KvAP) into photoswitchable lipid bilayers.
  • Utilizing blue and UV light to reversibly alter membrane thickness.
  • Measuring KvAP channel activity in response to light-induced membrane property changes.

Main Results:

  • Blue light illumination induced membrane thickening and increased KvAP channel activity.
  • UV light exposure reversed these effects, decreasing membrane thickness and KvAP activity.
  • Demonstrated a direct, reversible correlation between membrane thickness and Kv channel gating.

Conclusions:

  • Membrane thickness directly influences voltage-gated potassium channel gating by modulating voltage sensor-lipid interactions.
  • Light-activated membrane property modulation offers a non-genetic tool to control ion channel function.
  • Findings provide insights into remote control of neuronal excitability via membrane mechanics.