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

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

2.2K
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...
2.2K
Voltage-gated Ion Channels01:26

Voltage-gated Ion Channels

8.2K
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...
8.2K
Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

6.4K
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...
6.4K
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

3.4K
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
3.4K
Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

12.4K
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...
12.4K

You might also read

Related Articles

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

Sort by
Same author

Aberrant recovery of timescale-aligned amplitude balance links to symptoms and cognition in schizophrenia.

Translational psychiatry·2026
Same author

Preclinical Evaluation of [<sup>18</sup>F]JNJ-1: A Novel Positron Emission Tomography Ligand Targeting AMPAR/TARP γ8.

Molecular imaging and biology·2026
Same author

Large-scale brain dynamics are organized by a directional coordination hierarchy.

bioRxiv : the preprint server for biology·2026
Same author

APOE Isoform-Dependent Self-Association Measured by a Split-Luciferase Complementation Assay: Differential Effects of Disease-Risk and Protective Variants.

medRxiv : the preprint server for health sciences·2026
Same author

Crosstalk between NRP1 and autophagy in the tumor microenvironment: from molecular mechanisms to therapeutic targeting.

Frontiers in immunology·2026
Same author

The Carcinogenic Role of HMGB1 and NF-κB in Gastric Adenocarcinoma.

Digestive diseases and sciences·2026

Related Experiment Video

Updated: Jul 4, 2025

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

21.0K

Molecular determinants of ASIC1 modulation by divalent cations.

Yi Liu1, Jichun Ma2, Renee L DesJarlais2

  • 1Neuroscience Discovery, Janssen Research & Development, L.L.C., 3210 Merryfield Row, San Diego, CA, 92121, USA.

Scientific Reports
|January 28, 2024
PubMed
Summary

Divalent cations modulate acid-sensing ion channels (ASICs) by binding to an acidic pocket site. This binding is crucial for regulating ASIC1a channel gating, offering insights into channel modulation mechanisms.

More Related Videos

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry
11:32

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry

Published on: September 28, 2016

13.3K
Author Spotlight: Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

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

Published on: June 2, 2023

967

Related Experiment Videos

Last Updated: Jul 4, 2025

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

21.0K
Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry
11:32

Determination of the Relative Cell Surface and Total Expression of Recombinant Ion Channels Using Flow Cytometry

Published on: September 28, 2016

13.3K
Author Spotlight: Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
12:26

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

Published on: June 2, 2023

967

Area of Science:

  • Neuroscience
  • Ion Channel Physiology
  • Molecular Biology

Background:

  • Acid-sensing ion channels (ASICs) are proton-gated cation channels vital for nervous system functions.
  • ASIC gating is influenced by divalent cations and small molecules, but the mechanisms remain unclear.
  • Previous work identified small molecules modulating ASIC1a gating similarly to divalent cations.

Purpose of the Study:

  • To investigate the interaction between divalent cations and small molecules on ASIC1a.
  • To elucidate the molecular basis of divalent cation modulation on ASIC1a channel gating.

Main Methods:

  • Utilized mutational analysis of ASIC1a.
  • Examined the effects of divalent cations and identified small molecules on ASIC1a gating.
  • Investigated the binding site within the acidic pocket.

Main Results:

  • Divalent cation binding to an acidic pocket site is a key determinant of ASIC1a gating modulation.
  • The identified small molecules and divalent cations interact at this site.
  • Mutational studies confirmed the role of the acidic pocket in modulation.

Conclusions:

  • The acidic pocket is a critical site for divalent cation-mediated gating modulation of ASIC1a.
  • Understanding this interaction provides a molecular basis for ASIC channel regulation.
  • This research offers potential targets for therapeutic interventions involving ASICs.