Related Experiment Video
Updated: Jun 15, 2025
07:04
Long-range Channelrhodopsin-assisted Circuit Mapping of Inferior Colliculus Neurons with Blue and Red-shifted Channelrhodopsins
Published on: February 7, 2020
7.4K
Channelrhodopsins with distinct chromophores and binding patterns
Yuanyue Shan1,2, Liping Zhao1, Meiyu Chen1
1Laboratory of Cell Fate Control, School of Life Sciences, Westlake University, Hangzhou, China.
Nature Communications
|August 24, 2024
Summary
Channelrhodopsins (ChRs) are key optogenetic tools. New cryo-EM structures reveal diverse retinal binding in ChRs, impacting their function and inspiring future optogenetics.
Area of Science:
- Neuroscience
- Biophysics
- Structural Biology
Background:
- Channelrhodopsins (ChRs) are crucial optogenetic tools for neuroscience research.
- Their precise molecular mechanisms, particularly chromophore interactions, remain incompletely understood.
Purpose of the Study:
- To elucidate the structural basis of chromophore binding in different channelrhodopsins.
- To investigate how distinct chromophore-binding modes affect channelrhodopsin function in mammalian cells.
Main Methods:
- Cryo-electron microscopy (cryo-EM) to determine high-resolution structures.
- Functional characterization of channelrhodopsins in HEK293 cells.
- Analysis of chromophore interactions and photocurrents.
Main Results:
- ChR2 from C. reinhardtii binds an N-retinylidene-PE-like molecule in a novel lateral pocket, reducing light response.
- KCR1 from H. catenoides binds endogenous retinal in its canonical pocket.
- Exogenous ATR modulates KCR1 photocurrent, affecting both wild-type and a leaky mutant.
Conclusions:
- Channelrhodopsins exhibit diverse chromophore binding patterns and pocket utilization in mammalian cells.
- These findings reveal mechanistic insights into ChR function and suggest avenues for engineering next-generation optogenetic tools.
More Related Videos
08:39Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins
Published on: May 22, 2017
17.1K
11:08Two Peeling Methods for the Isolation of Photoreceptor Cell Compartments in the Mouse Retina for Protein Analysis
Published on: December 7, 2021
3.1K
Related Concept Videos
01:11Channel Rhodopsins
2.5K
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,...
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
2.5K
01:22Photoreceptors and Visual Pathways
5.9K
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,...
5.9K
01:21G-Protein Gated Ion Channels
4.5K
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...
Sensory...
4.5K
01:15G Protein-coupled Receptors
11.6K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
11.6K
01:30Transducer Mechanism: G Protein–Coupled Receptors
1.9K
G Protein–Coupled Receptors (GPCRs) are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to various stimuli. GPCRs regulate critical physiological pathways and are excellent drug targets for treating diseases such as diabetes, cancer, obesity, depression, or Alzheimer's. Nearly 35% of approved drugs implement their therapeutic effects by selectively interacting with specific GPCRs.
GPCRs are also called heptahelical,...
GPCRs are also called heptahelical,...
1.9K
01:29The Photochemical Reaction Center
4.1K
Reaction centers are pigment-protein complexes that initiate energy conversion from photons to chemical entities. Therefore, photochemical reaction center is a more appropriate term that describes these complexes. The Nobel laureates Robert Emerson and William Arnold provided the first experimental evidence of photochemical reaction centers by demonstrating the participation of nearly 2,500 chlorophyll molecules for the release of just one molecule of oxygen. Despite thousands of photosynthetic...
4.1K