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

Channel Rhodopsins01:11

Channel Rhodopsins

2.9K
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,...
2.9K
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

5.2K
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...
5.2K
Photoreceptors and Visual Pathways01:22

Photoreceptors and Visual Pathways

8.0K
At the molecular level, visual signals trigger transformations in photopigment molecules, resulting in changes in the photoreceptor cell's membrane potential. The photon's energy level is denoted by its wavelength, with each specific wavelength of visible light associated with a distinct color. The spectral range of visible light, classified as electromagnetic radiation, spans from 380 to 720 nm. Electromagnetic radiation wavelengths exceeding 720 nm fall under the infrared category,...
8.0K
Anatomy of the Eyeball01:20

Anatomy of the Eyeball

8.9K
The eye is a spherical, hollow structure composed of three tissue layers. The outer layer — the fibrous tunic, comprises the sclera — a white structure — and the cornea, which is transparent. The sclera encompasses some of the ocular surface, most of which is not visible. However, the 'white of the eye' is distinctively visible in humans compared to other species. The cornea, a clear covering at the front of the eye, enables light penetration. The eye's middle...
8.9K
Electrochemical Gradient and Channel Proteins: An Overview01:21

Electrochemical Gradient and Channel Proteins: An Overview

3.8K
An electrochemical gradient is a fundamental concept in biology and chemistry. It regulates the movement of ions across cell membranes. This movement is influenced by two factors:
The electrical gradient: The electrical gradient across cell membranes refers to the difference in electric charge between the inside and outside of a cell.  This difference drives the movement of ions towards or away from the cells. For instance, if the inside of the cell is more negatively charged relative to...
3.8K
Structure of Cadherins01:25

Structure of Cadherins

4.2K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
4.2K

You might also read

Related Articles

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

Sort by
Same author

Structural insights into spectral tuning and retinal exchange in cone visual pigments.

Science (New York, N.Y.)·2026
Same author

Illuminating the molecular basis of human daylight vision.

Science (New York, N.Y.)·2026
Same author

The dynamic basis of G-protein recognition and activation by a GPCR.

Nature·2026
Same author

Structural Changes in the Retinal Chromophore and Ion-Conducting Pathway of an Anion Channelrhodopsin <i>Gt</i>ACR1.

The journal of physical chemistry letters·2025
Same author

Structural insights into lipid chain-length selectivity and allosteric regulation of FFA2.

Nature communications·2025
Same author

Structural basis for ion selectivity in potassium-selective channelrhodopsins.

Cell·2023

Related Experiment Video

Updated: Nov 23, 2025

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
08:39

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

Published on: May 22, 2017

17.7K

Structure-Function Relationship of Channelrhodopsins.

Hideaki E Kato1

  • 1Komaba Institute for Science, The University of Tokyo, Tokyo, Japan. hekato@bio.c.u-tokyo.ac.jp.

Advances in Experimental Medicine and Biology
|January 5, 2021
PubMed
Summary
This summary is machine-generated.

Channelrhodopsins (ChRs) are light-activated ion channels crucial for optogenetics. Recent structural and biophysical studies have significantly advanced our understanding of their light-gated ion conduction mechanisms.

Keywords:
ChannelrhodopsinOptogeneticsStructural biologyStructure-guided engineeringStructure-guided mining

More Related Videos

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.2K
Long-range Channelrhodopsin-assisted Circuit Mapping of Inferior Colliculus Neurons with Blue and Red-shifted Channelrhodopsins
07:04

Long-range Channelrhodopsin-assisted Circuit Mapping of Inferior Colliculus Neurons with Blue and Red-shifted Channelrhodopsins

Published on: February 7, 2020

7.6K

Related Experiment Videos

Last Updated: Nov 23, 2025

Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
08:39

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

Published on: May 22, 2017

17.7K
Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
10:03

Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

Published on: June 27, 2014

18.2K
Long-range Channelrhodopsin-assisted Circuit Mapping of Inferior Colliculus Neurons with Blue and Red-shifted Channelrhodopsins
07:04

Long-range Channelrhodopsin-assisted Circuit Mapping of Inferior Colliculus Neurons with Blue and Red-shifted Channelrhodopsins

Published on: February 7, 2020

7.6K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Optogenetics

Background:

  • Ion-translocating rhodopsins, particularly channelrhodopsins (ChRs), are key tools in optogenetics for light-controlled cellular membrane potential modulation.
  • The discovery of the first ChR in 2002 paved the way for optogenetic technology.
  • Rhodopsin family proteins share fundamental structural and functional characteristics.

Purpose of the Study:

  • To provide a comprehensive overview of rhodopsin family proteins and the development of optogenetics.
  • To elucidate the structure-function relationships of ChRs through comparative analysis of cation and anion ChR crystal structures.
  • To discuss future directions in ChR research and optogenetic tool advancement.

Main Methods:

  • Structural determination of cation and anion channelrhodopsins (ChRs).
  • Biophysical and spectroscopic analyses of ChR function.
  • Computational studies to understand light-gated ion conduction.

Main Results:

  • Significant advancements in understanding the molecular mechanisms of light-gated ion conduction in ChRs.
  • Comparative insights into the structural differences and functional implications of cation and anion ChRs.
  • Detailed exploration of the structure-function relationship in ChRs.

Conclusions:

  • Recent structural and biophysical studies have greatly enhanced the understanding of channelrhodopsin (ChR) mechanisms.
  • Comparative analysis of ChR structures provides critical insights into ion conduction.
  • Future research aims to further refine ChR properties for advanced optogenetic applications.