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Channelrhodopsin-2, a directly light-gated cation-selective membrane channel
Open accessAbstract
Microbial-type rhodopsins are found in archaea, prokaryotes, and eukaryotes. Some of them represent membrane ion transport proteins such as bacteriorhodopsin, a light-driven proton pump, or channelrhodopsin-1 (ChR1), a recently identified light-gated proton channel from the green alga Chlamydomonas reinhardtii . ChR1 and ChR2, a related microbial-type rhodopsin from C. reinhardtii , were shown to be involved in generation of photocurrents of this green alga. We demonstrate by functional expression, both in oocytes of Xenopus laevis and mammalian cells, that ChR2 is a directly light-switched cation-selective ion channel. This channel opens rapidly after absorption of a photon to generate a large permeability for monovalent and divalent cations. ChR2 desensitizes in continuous light to a smaller steady-state conductance. Recovery from desensitization is accelerated by extracellular H + and negative membrane potential, whereas closing of the ChR2 ion channel is decelerated by intracellular H + . ChR2 is expressed mainly in C. reinhardtii under low-light conditions, suggesting involvement in photoreception in dark-adapted cells. The predicted seven-transmembrane α helices of ChR2 are characteristic for G protein-coupled receptors but reflect a different motif for a cation-selective ion channel. Finally, we demonstrate that ChR2 may be used to depolarize small or large cells, simply by illumination.
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Self-citation
Metadata
- Authors
- Nagel, G., Szellas, T., Huhn, W., Kateriya, S., Adeishvili, N., Berthold, P., Ollig, D., Hegemann, P., & Bamberg, E.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-11-13
- Volume
- 100
- Issue
- 24
- Pages
- 13940-13945
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2159423248
- Cited by
- 2,663
- References
- 2
- FWCI
- 4.33
- Type
- journal article
- Language
- en
- Open access
- green
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