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

3.6K
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...
3.6K
Electrochemical Gradient and Channel Proteins: An Overview01:21

Electrochemical Gradient and Channel Proteins: An Overview

4.1K
An electrochemical gradient is a fundamental concept in biology and chemistry. It regulates the movement of ions across cell membranes. This movement is influenced by two factors:
The electrical gradient: The electrical gradient across cell membranes refers to the difference in electric charge between the inside and outside of a cell.  This difference drives the movement of ions towards or away from the cells. For instance, if the inside of the cell is more negatively charged relative to...
4.1K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

7.4K
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...
7.4K
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

13.8K
Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
13.8K
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

8.5K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
8.5K
Potentiometry: Membrane Electrodes01:15

Potentiometry: Membrane Electrodes

1.4K
Membrane electrodes, also known as p-ion electrodes, use membranes that selectively interact with free analyte ions, generating a potential difference across the membrane. The resulting membrane potential, known as the asymmetry potential, is not zero even when analyte concentrations on both sides of the membrane are equal. The membrane's response is typically not selective to a single analyte but proportional to the concentration of all ions in the sample solution capable of interacting at...
1.4K

You might also read

Related Articles

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

Sort by
Same author

Reply to Rattanapitoon et al.

Pain·2026
Same author

Catalysis of Native Chemical Ligation and Expressed Protein Ligation by Alkylselenols.

JACS Au·2025
Same author

Precise dynamic control of tissue oxygenation during brain slice electrophysiology.

American journal of physiology. Cell physiology·2025
Same author

Synaptic proteome diversity is shaped by the levels of glutamate receptors and their regulatory proteins.

Nature communications·2025
Same author

Efficacy and safety of the Ca<sub>v</sub>2.2 blocker Ziconotide in pain: a meta-analysis and systematic review.

Pain reports·2025
Same author

Long-lasting behavioral, molecular and functional connectivity alterations after chronic THC exposure during adolescence in mice.

Progress in neuro-psychopharmacology & biological psychiatry·2025

Related Experiment Video

Updated: Dec 20, 2025

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties
12:20

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

Published on: November 3, 2008

9.7K

AMPAR/TARP stoichiometry differentially modulates channel properties.

Federico Miguez-Cabello1, Nuria Sánchez-Fernández1, Natalia Yefimenko1

  • 1Laboratori de Neurofisiologia, Departament de Biomedicina, Facultat de Medicina i Ciències de la Salut, Institut de Neurociències, Universitat de Barcelona, Barcelona, Spain.

Elife
|May 27, 2020
PubMed
Summary

The stoichiometry of TARP γ2 binding to AMPARs significantly impacts channel properties, with full saturation required for key TARP-induced characteristics. Differences were observed between calcium-permeable and impermeable AMPARs, suggesting two γ2 molecules at cerebellar granule cell receptors.

Keywords:
AMPARTARPcerebellar granule cellschannel conductancehumanmouseneuroscienceout-side outstoichiometry

More Related Videos

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

13.8K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.3K

Related Experiment Videos

Last Updated: Dec 20, 2025

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties
12:20

Single Molecule Methods for Monitoring Changes in Bilayer Elastic Properties

Published on: November 3, 2008

9.7K
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

13.8K
Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
11:53

Purification and Reconstitution of TRPV1 for Spectroscopic Analysis

Published on: July 3, 2018

8.3K

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biophysics

Background:

  • AMPA receptors (AMPARs) mediate fast synaptic transmission.
  • Auxiliary subunits, such as TARPs, modulate AMPAR function.
  • The stoichiometric relationship between AMPARs and TARPs is poorly understood.

Purpose of the Study:

  • To investigate the stoichiometry-dependent modulation of AMPARs by TARP γ2.
  • To explore differences in modulation between calcium-permeable and impermeable AMPARs.
  • To determine the stoichiometry of γ2 at endogenous AMPARs in mouse cerebellar granule cells.

Main Methods:

  • Electrophysiological recordings of recombinant AMPARs and TARP γ2.
  • Mutagenesis studies to assess the role of γ2 positioning.
  • Comparison with endogenous AMPAR currents from mouse cerebellar granule cells.

Main Results:

  • AMPARs exhibit stoichiometry-dependent modulation by TARP γ2.
  • Full saturation with γ2 is necessary for typical TARP-induced channel conductance.
  • Distinct stoichiometric modulation patterns exist for calcium-permeable versus impermeable AMPARs.
  • γ2 positioning within heteromeric AMPARs influences TARP-dependent features.
  • A stoichiometry of two γ2 molecules per somatic AMPAR was inferred in mouse cerebellar granule cells.

Conclusions:

  • TARP γ2 stoichiometry critically influences AMPAR channel properties.
  • The number and positioning of γ2 subunits are key determinants of AMPAR function.
  • Endogenous AMPARs in cerebellar granule cells likely contain two γ2 subunits.