ArticlePhotochemistry and photobiology
Diversity of Chlamydomonas channelrhodopsins.
Article in Photochemistry and photobiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 66 citations in OpenAlex.
- A red-light gate for a cation channel: The conducting state of channelrhodopsin-1 from Chlamydomonas augustae.Biophysical journal · 2026Article
- Optogenetic engineering for ion channel modulation.Current opinion in chemical biology · 2025Review
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- Preference of Proteomonas sulcata anion channelrhodopsin for NOScientific reports · 2021Article
- Emerging Diversity of Channelrhodopsins and Their Structure-Function Relationships.Frontiers in cellular neuroscience · 2021Review
- Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases.Frontiers in molecular biosciences · 2021Review
- Structure-Function Relationship of Channelrhodopsins.Advances in experimental medicine and biology · 2021Review
- Novel optogenetics tool: Gt_CCR4, a light-gated cation channel with high reactivity to weak light.Biophysical reviews · 2020Review
- Ultrafast Backbone Protonation in Channelrhodopsin-1 Captured by Polarization Resolved Fs Vis-pump-IR-Probe Spectroscopy and Computational Methods.Molecules (Basel, Switzerland) · 2020Article
- Crystal structure of the red light-activated channelrhodopsin Chrimson.Nature communications · 2018Article
- Conversion of microbial rhodopsins: insights into functionally essential elements and rational protein engineering.Biophysical reviews · 2017Review
- Molecular determinants of proton selectivity and gating in the red-light activated channelrhodopsin Chrimson.Scientific reports · 2017Article
- Reaction dynamics of the chimeric channelrhodopsin C1C2.Scientific reports · 2017Article
- Whole-cell Patch-clamp Recordings for Electrophysiological Determination of Ion Selectivity in Channelrhodopsins.Journal of visualized experiments : JoVE · 2017Article
- Structure-guided SCHEMA recombination generates diverse chimeric channelrhodopsins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The Expanding Family of Natural Anion Channelrhodopsins Reveals Large Variations in Kinetics, Conductance, and Spectral Sensitivity.Scientific reports · 2017Article
- Femtosecond infrared spectroscopy of channelrhodopsin-1 chromophore isomerization.Structural dynamics (Melville, N.Y.) · 2016Article
- Resonance Raman Study of an Anion Channelrhodopsin: Effects of Mutations near the Retinylidene Schiff Base.Biochemistry · 2016Article
- Recent advances in engineering microbial rhodopsins for optogenetics.Current opinion in structural biology · 2015Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Channelrhodopsins act as photoreceptors for control of motility behavior in flagellates and are widely used as genetically targeted tools to optically manipulate the membrane potential of specific cell populations ("optogenetics"). The first two channelrhodopsins were obtained from the model organism Chlamydomonas reinhardtii (CrChR1 and CrChR2). By homology cloning we identified three new channelrhodopsin sequences from the same genus, CaChR1, CyChR1 and CraChR2, from C. augustae, C. yellowstonensis and C. raudensis, respectively. CaChR1 and CyChR1 were functionally expressed in HEK293 cells, where they acted as light-gated ion channels similar to CrChR1. However, both, which are similar to each other, differed from CrChR1 in current kinetics, inactivation, light intensity dependence, spectral sensitivity and dependence on the external pH. These results show that extensive channelrhodopsin diversity exists even within the same genus, Chlamydomonas. The maximal spectral sensitivity of CaChR1 was at 520 nm at pH 7.4, about 40 nm redshifted as compared to that of CrChR1 under the same conditions. CaChR1 was successfully expressed in Pichia pastoris and exhibited an absorption spectrum identical to the action spectrum of CaChR1-generated photocurrents. The redshifted spectra and the lack of fast inactivation in CaChR1- and CyChR1-generated currents are features desirable for optogenetics applications.
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