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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...

Mechanically-gated Ion Channels

Mechanically-gated Ion Channels

Voltage-gated Ion Channels

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 Channels

Voltage-gated Ion Channels

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....

Non-gated Ion Channels

Non-gated Ion Channels

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Related Experiment Video

Updated: Apr 25, 2026

Controllable Ion Channel Expression through Inducible Transient Transfection

Controllable Ion Channel Expression through Inducible Transient Transfection

Published on: February 17, 2017

Building a temperature-sensitive ion channel.

Ming-Feng Tsai¹, Christopher Miller¹

¹Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02453, USA.

|August 30, 2014

Summary

This summary is machine-generated.

Researchers engineered temperature-insensitive ion channels to become cold- or heat-responsive. This protein engineering approach reveals key principles of temperature-gating and environmental responsiveness in ion channels.

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Last Updated: Apr 25, 2026

Controllable Ion Channel Expression through Inducible Transient Transfection

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Published on: February 17, 2017

One-channel Cell-attached Patch-clamp Recording

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Published on: June 9, 2014

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

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Published on: April 19, 2021

Area of Science:

Biophysics
Molecular Biology
Ion Channel Physiology

Background:

Understanding temperature-sensitive ion channel gating is crucial for cellular function.
The molecular mechanisms underlying thermosensation remain largely unknown.
Voltage-gated channels typically lack inherent temperature sensitivity.

Purpose of the Study:

To investigate the biophysical principles of temperature-sensitive ion channel gating.
To engineer a temperature-insensitive channel to respond to thermal stimuli.
To develop a model for molecular thermosensation in ion channels.

Main Methods:

Utilized a protein engineering strategy.
Modified a voltage-gated ion channel to introduce temperature sensitivity.
Assessed channel gating in response to cold and heat stimuli.

Main Results:

Successfully rendered a temperature-insensitive channel responsive to cold and heat.
Identified key structural or functional elements enabling temperature-gating.
Established a plausible model for the molecular basis of thermosensation.

Conclusions:

Protein engineering can confer temperature sensitivity to ion channels.
Revealed fundamental principles governing temperature-gated ion channel function.
Provides insights into molecular mechanisms of environmental sensing.