ArticleNature communications2022
Cryo-EM structures of the channelrhodopsin ChRmine in lipid nanodiscs.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- Channel gating in bacteriorhodopsin-like channelrhodopsins with contrasting KBiophysical journal · 2026Article
- A red-light gate for a cation channel: The conducting state of channelrhodopsin-1 from Chlamydomonas augustae.Biophysical journal · 2026Article
- Cryo-EM structure of human AQP11 reveals a trimeric architecture with a large pore.Science advances · 2026Article
- The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Roadmap for direct and indirect translation of optogenetics into discoveries and therapies for humans.Nature neuroscience · 2025Review
- Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- Optogenetic restoration of high-sensitivity vision using ChRmine- and ChroME-based channelrhodopsins.Scientific reports · 2025Article
- Pore-Opening and Ion-Conduction Mechanism in Channelrhodopsins C1C2, ChR2, and iChloC by Computational Electrophysiology and Constant-pH Simulations.Journal of chemical information and modeling · 2025Article
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Nanodiscs remain indispensable for Cryo-EM studies of membrane proteins.Current opinion in structural biology · 2025Review
- Structural insights into light-gating of potassium-selective channelrhodopsin.Nature communications · 2025Article
- Structural insights into CXCR4 modulation and oligomerization.Nature structural & molecular biology · 2025Article
- Channelrhodopsins with distinct chromophores and binding patterns.Nature communications · 2024Article
- Channel Gating in Kalium Channelrhodopsin Slow Mutants.Journal of molecular biology · 2024Article
- Crystallographic insights into lipid-membrane protein interactions in microbial rhodopsins.Frontiers in molecular biosciences · 2024Article
- LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins.Nature communications · 2023Article
- Article
- Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting KNature communications · 2023Article
- A light-gated cation channel with high reactivity to weak light.Scientific reports · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Microbial channelrhodopsins are light-gated ion channels widely used for optogenetic manipulation of neuronal activity. ChRmine is a bacteriorhodopsin-like cation channelrhodopsin (BCCR) more closely related to ion pump rhodopsins than other channelrhodopsins. ChRmine displays unique properties favorable for optogenetics including high light sensitivity, a broad, red-shifted activation spectrum, cation selectivity, and large photocurrents, while its slow closing kinetics impedes some applications. The structural basis for ChRmine function, or that of any other BCCR, is unknown. Here, we present cryo-EM structures of ChRmine in lipid nanodiscs in apo (opsin) and retinal-bound (rhodopsin) forms. The structures reveal an unprecedented trimeric architecture with a lipid filled central pore. Large electronegative cavities on either side of the membrane facilitate high conductance and selectivity for cations over protons. The retinal binding pocket structure suggests channel properties could be tuned with mutations and we identify ChRmine variants with ten-fold decreased and two-fold increased closing rates. A T119A mutant shows favorable properties relative to wild-type and previously reported ChRmine variants for optogenetics. These results provide insight into structural features that generate an ultra-potent microbial opsin and provide a platform for rational engineering of channelrhodopsins with improved properties that could expand the scale, depth, and precision of optogenetic experiments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.