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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.
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...

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Related Experiment Video

Updated: Apr 11, 2026

Light-Controlled Fermentations for Microbial Chemical and Protein Production

Light-Controlled Fermentations for Microbial Chemical and Protein Production

Published on: March 22, 2022

Recent advances in engineering microbial rhodopsins for optogenetics.

R Scott McIsaac^1,2, Claire N Bedbrook³, Frances H Arnold^1,3

¹Division of Chemistry and Chemical Engineering, Mail Code 210-41, California Institute of Technology, Pasadena, California, United States of America.

Current Opinion in Structural Biology

|June 4, 2015

Summary

This summary is machine-generated.

Protein engineering enhances microbial rhodopsins for optogenetics. These engineered proteins act as sensors and actuators for neuronal activity, improving optogenetic tools and revealing structure-function insights.

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Area of Science:

Biochemistry and Molecular Biology
Neuroscience
Biophysics

Background:

Microbial rhodopsins are versatile membrane proteins.
They function as light-driven ion pumps and sensors.
Optogenetics utilizes these proteins to control or monitor neuronal activity.

Purpose of the Study:

To review protein engineering strategies for microbial rhodopsins.
To highlight advancements in developing optogenetic tools based on these proteins.
To discuss the insights gained into rhodopsin structure-function relationships.

Main Methods:

Protein engineering approaches including chimeragenesis, structure-guided mutagenesis, and directed evolution.
Characterization of engineered rhodopsin variants for altered properties.
Application of engineered rhodopsins in optogenetic studies.

Main Results:

Successful generation of microbial rhodopsin variants with improved optogenetic properties.
Demonstrated ability to tune absorption wavelength, ion specificity, and fluorescence.
Development of enhanced tools for sensing and actuating neuronal activity.

Conclusions:

Protein engineering is a powerful strategy for advancing microbial rhodopsins in optogenetics.
These engineered rhodopsins offer improved performance and novel functionalities.
Further research can yield deeper understanding of rhodopsin mechanisms and applications.