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Mechanically-gated Ion Channels

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...

Non-gated Ion Channels

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....

G-Protein Gated Ion Channels

G-Protein Gated Ion Channels

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...

Ligand-Gated Ion Channel Receptor: Gating Mechanism

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...

Ligand-gated Ion Channels

Ligand-gated Ion Channels

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...

Thermosensation

Thermosensation

Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...

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Related Experiment Video

Updated: Jul 9, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

Targeting Ion Channel TRPM4.

Barbara Preti¹, Jean-Sébastien Rougier², Irida Papapostolou²

¹Institute if Biochemistry and Molecular Medicine, University of Bern.

|December 9, 2023

Summary

This summary is machine-generated.

Researchers identified novel small molecules that inhibit the TRPM4 ion channel. These TRPM4 inhibitors were used to explore the channel's role in heart disease, immune disorders, and cancer.

Keywords:

Cancer Cardiac disease Small-molecule inhibitors TRPM4

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Related Experiment Videos

Last Updated: Jul 9, 2025

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Yeast Luminometric and Xenopus Oocyte Electrophysiological Examinations of the Molecular Mechanosensitivity of TRPV4

Published on: December 31, 2013

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

Controllable Ion Channel Expression through Inducible Transient Transfection

Controllable Ion Channel Expression through Inducible Transient Transfection

Published on: February 17, 2017

Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

The transient receptor potential melastatin 4 (TRPM4) ion channel is widely present in the body.
TRPM4 dysfunction or mutations are associated with various diseases.
Understanding TRPM4's role is crucial for developing new therapeutic strategies.

Purpose of the Study:

To identify and characterize small molecule inhibitors of the TRPM4 ion channel.
To investigate the involvement of TRPM4 in the pathophysiology of cardiac conditions, immune diseases, and cancer.

Main Methods:

High-throughput screening to identify TRPM4 inhibitors.
Biochemical assays to determine inhibitor potency (low µM range).
Molecular biology techniques and functional assays to study TRPM4 in disease models.

Main Results:

Identification of novel small molecules with low micromolar inhibitory activity against TRPM4.
Demonstration of TRPM4's contribution to cardiac conditions, immune diseases, and cancer.
Establishment of a toolkit for further TRPM4 research.

Conclusions:

TRPM4 is a druggable target for various diseases.
Novel TRPM4 inhibitors provide valuable tools for studying TRPM4-related pathophysiology.
Targeting TRPM4 may offer therapeutic potential in cardiovascular, immunological, and oncological conditions.