ArticleProceedings of the National Academy of Sciences of the United States of America2015
Gating mechanisms of a natural anion channelrhodopsin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Tutorial: Transient Absorption Spectroscopy for Probing Ultrafast Dynamics.ACS physical chemistry Au · 2026Article
- Channel gating in bacteriorhodopsin-like channelrhodopsins with contrasting KBiophysical journal · 2026Article
- Reward-driven cerebellar climbing fiber activity influences both neural and behavioral learning.Current biology : CB · 2025Article
- Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Reward-driven cerebellar climbing fiber activity influences both neural and behavioral learning.bioRxiv : the preprint server for biology · 2025Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- Combined Mutational and Spectroscopic Study on the Calcium-Related Kinetic Effects on the VirChR1 Photocycle.The journal of physical chemistry. B · 2025Article
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Parallel photocycle kinetic model of anion channelrhodopsin GtACR1 function.Biophysical journal · 2024Article
- Optogenetic Determination of Dynamic and Cell-Type-Specific Inhibitory Reversal Potentials.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- The open channel state in anion channelrhodopsin GtACR1 is a red-absorbing intermediate.Biophysical journal · 2024Article
- Isospectral intermediates in the photochemical reaction cycle of anion channelrhodopsin GtACR1.Biophysical journal · 2023Article
- Sequential absorption of two photons creates a bistable form of RubyACR responsible for its strong desensitization.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cross-modal modulation gates nociceptive inputs in Drosophila.Current biology : CB · 2023Article
- Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing.Communications biology · 2022Article
- Kalium channelrhodopsins are natural light-gated potassium channels that mediate optogenetic inhibition.Nature neuroscience · 2022Article
- Optogenetic Control of Heart Rhythm: Lightly Guiding the Cardiac Pace.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022Article
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4 authors.
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Abstract
Anion channelrhodopsins (ACRs) are a class of light-gated channels recently identified in cryptophyte algae that provide unprecedented fast and powerful hyperpolarizing tools for optogenetics. Analysis of photocurrents generated by Guillardia theta ACR 1 (GtACR1) and its mutants in response to laser flashes showed that GtACR1 gating comprises two separate mechanisms with opposite dependencies on the membrane voltage and pH and involving different amino acid residues. The first mechanism, characterized by slow opening and fast closing of the channel, is regulated by Glu-68. Neutralization of this residue (the E68Q mutation) specifically suppressed this first mechanism, but did not eliminate it completely at high pH. Our data indicate the involvement of another, yet-unidentified pH-sensitive group X. Introducing a positive charge at the Glu-68 site (the E68R mutation) inverted the channel gating so that it was open in the dark and closed in the light, without altering its ion selectivity. The second mechanism, characterized by fast opening and slow closing of the channel, was not substantially affected by the E68Q mutation, but was controlled by Cys-102. The C102A mutation reduced the rate of channel closing by the second mechanism by ∼100-fold, whereas it had only a twofold effect on the rate of the first. The results show that anion conductance by ACRs has a fundamentally different structural basis than the relatively well studied conductance by cation channelrhodopsins (CCRs), not attributable to simply a modification of the CCR selectivity filter.
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