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Channel Rhodopsins

Channel Rhodopsins

Most organisms use photoreceptors to sense and respond to light. Examples of photoreceptors include bacteriorhodopsins and bacteriophytochromes in some bacteria, phytochromes in plants, and rhodopsins in the photoreceptor cells of the vertebral retina. The light-sensitive property of these receptors is because of the bound chromophores, such as bilin in the phytochromes and retinal in the rhodopsins.
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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...

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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...

Non-gated Ion Channels

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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.
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Ligand-gated Ion Channels

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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...

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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...

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Related Experiment Video

Updated: Jan 11, 2026

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

Published on: May 22, 2017

Stabilized Ion Selectivity Corrects Activation Drift in Kalium Channelrhodopsins.

Xiao Duan¹, Chong Zhang¹, Stanislav Ott²

¹Department of Neurophysiology, Institute of Physiology, University Wuerzburg, 97070, Wuerzburg, Germany.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)

|November 10, 2025

Summary

New KCR1-C29D optogenetic tools reliably silence neurons by maintaining potassium selectivity, unlike other variants. This breakthrough offers stable, effective neural circuit inhibition across species and conditions.

Keywords:

Kalium channelrhodopsin (KCR)depolarization and hyperpolarization neuronal activation neuronal inhibition optogenetics

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Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins

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Published on: May 22, 2017

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Recapitulation of an Ion Channel IV Curve Using Frequency Components

Recapitulation of an Ion Channel IV Curve Using Frequency Components

Published on: February 8, 2011

Area of Science:

Neuroscience
Optogenetics
Molecular Biology

Background:

Optogenetic inhibition of neuronal activity is crucial for neuroscience research.
Potassium-selective channelrhodopsins (KCRs) are promising for neuronal silencing but often suffer from ion selectivity shifts under prolonged illumination, limiting their efficacy.
This ion selectivity shift can lead to unintended neuronal excitation, hindering reliable circuit silencing.

Purpose of the Study:

To identify and characterize KCR variants with stable ion selectivity for reliable optogenetic neuronal inhibition.
To evaluate the performance of KCR variants in silencing neural circuits across different species and conditions.
To establish improved design criteria for next-generation optogenetic inhibitory tools.

Main Methods:

Behavioral and electrophysiological analyses were performed in model organisms, including Drosophila and Caenorhabditis elegans.
The ion selectivity (K+/Na+ permeability ratio) and its stability over time under illumination were assessed for various KCR variants.
In vivo inhibition efficacy of KCR variants was tested across different cell types and illumination conditions.

Main Results:

The KCR1-C29D mutant demonstrated a high and exceptionally stable K+/Na+ permeability ratio during illumination compared to other tested KCR variants.
Unlike other variants that often induced excitatory responses, KCR1-C29D consistently achieved robust in vivo neuronal inhibition.
The stability of ion selectivity was identified as a critical factor determining the effectiveness of KCRs for silencing neural circuits.

Conclusions:

KCR1-C29D is a superior and reliable optogenetic tool for neuronal inhibition due to its stable ion selectivity.
This study addresses a significant limitation in KCR optogenetics, providing a dependable method for silencing neural circuits.
The findings emphasize the importance of ion selectivity stability in designing effective future optogenetic tools.