ArticleCommunications biology2021
Specific residues in the cytoplasmic domain modulate photocurrent kinetics of channelrhodopsin from Klebsormidium nitens.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Article
- Blue-shifted ancyromonad channelrhodopsins for multiplex optogenetics.bioRxiv : the preprint server for biology · 2025Article
- Cryo-EM structure of a blue-shifted channelrhodopsin from Klebsormidium nitens.Nature communications · 2025Article
- HulaChrimson: A Chrimson-like cation channelrhodopsin discovered using freshwater metatranscriptomics from Lake Hula.Biophysics and physicobiology · 2025Article
- Environmental Proteomics Elucidates Phototrophic Biofilm Responses to Ornamental Lighting on Stone-built Heritage.Microbial ecology · 2024Article
- Article
- Article
- A light-gated cation channel with high reactivity to weak light.Scientific reports · 2023Article
- Recent advances in signaling and activation mechanism in microbial rhodopsins: Report for the session 6 at the 19Biophysics and physicobiology · 2023Article
- Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023Article
- A kinetic-optimized CoChR variant with enhanced high-frequency spiking fidelity.Biophysical journal · 2022Article
- Engineering rhodopsins' activation spectra using a FRET-based approach.Biophysical journal · 2022Article
- Emerging Diversity of Channelrhodopsins and Their Structure-Function Relationships.Frontiers in cellular neuroscience · 2021Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Channelrhodopsins (ChRs) are light-gated ion channels extensively applied as optogenetics tools for manipulating neuronal activity. All currently known ChRs comprise a large cytoplasmic domain, whose function is elusive. Here, we report the cation channel properties of KnChR, one of the photoreceptors from a filamentous terrestrial alga Klebsormidium nitens, and demonstrate that the cytoplasmic domain of KnChR modulates the ion channel properties. KnChR is constituted of a 7-transmembrane domain forming a channel pore, followed by a C-terminus moiety encoding a peptidoglycan binding domain (FimV). Notably, the channel closure rate was affected by the C-terminus moiety. Truncation of the moiety to various lengths prolonged the channel open lifetime by more than 10-fold. Two Arginine residues (R287 and R291) are crucial for altering the photocurrent kinetics. We propose that electrostatic interaction between the rhodopsin domain and the C-terminus domain accelerates the channel kinetics. Additionally, maximal sensitivity was exhibited at 430 and 460 nm, the former making KnChR one of the most blue-shifted ChRs characterized thus far, serving as a novel prototype for studying the molecular mechanism of color tuning of the ChRs. Furthermore, KnChR would expand the optogenetics tool kit, especially for dual light applications when short-wavelength excitation is required.
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