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Combining different ion-selective channelrhodopsins to control water flux by light
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Abstract
Water transport through water channels, aquaporins (AQPs), is vital for many physiological processes including epithelial fluid secretion, cell migration and adipocyte metabolism. Water flux through AQPs is driven by the osmotic gradient that results from concentration differences of solutes including ions. Here, we developed a novel optogenetic toolkit that combines the light-gated anion channel Gt ACR1 either with the light-gated K + channel Hc KCR1 or the new Na + channelrhodopsin Hc NCR1 with high Na + permeability, to manipulate water transport in Xenopus oocytes non-invasively. Water efflux through AQP was achieved by light-activating K + and Cl - efflux through Hc KCR1 and Gt ACR1. Contrarily, when Gt ACR1 was co-expressed with Hc NCR1, inward movement of Na + and Cl - was light-triggered, and the resulting osmotic gradient led to water influx through AQP1. In sum, we demonstrate a novel optogenetic strategy to manipulate water movement into or out of Xenopus oocytes non-invasively. This approach provides a new avenue to interfere with water homeostasis as a means to study related biological phenomena across cell types and organisms.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Research works printed but not linked: 29
- Baumgart F, Rossi A, Verkman AS (2011) Light inactivation of water transport and protein–protein interactions of aquaporin–Killer Red chimeras. J Gen Physiol 139:83–90. https://doi.org/10.1085/jgp.201110712 · DOI
- Beck S, Yu-Strzelczyk J, Pauls D, Constantin OM, Gee CE, Ehmann N, Kittel RJ, Nagel G, Gao S (2018) Synthetic light-activated ion channels for optogenetic activation and inhibition. Front Neurosci 12:643. https://doi.org/10.3389/fnins.2018.00643 · DOI
- Bernal Sierra YA, Rost BR, Pofahl M, Fernandes AM, Kopton RA, Moser S, Holtkamp D, Masala N, Beed P, Tukker JJ, Oldani S, Bonigk W, Kohl P, Baier H, Schneider-Warme F, Hegemann P, Beck H, Seifert R, Schmitz D (2018) Potassium channel-based optogenetic silencing. Nat Commun 9:4611. https://doi.org/10.1038/s41467-018-07038-8 · DOI
- Boton R, Dascal N, Gillo B, Lass Y (1989) Two calcium-activated chloride conductances in Xenopus laevis oocytes permeabilized with the ionophore A23187. J Physiol 408:511–534. https://doi.org/10.1113/jphysiol.1989.sp017473 · DOI
- Chen F, Duan X, Yu Y, Yang S, Chen Y, Gee CE, Nagel G, Zhang K, Gao S, Shen Y (2022) Visual function restoration with a highly sensitive and fast Channelrhodopsin in blind mice. Signal Transduct Target Ther 7:104. https://doi.org/10.1038/s41392-022-00935-x · DOI
- Day RE, Kitchen P, Owen DS, Bland C, Marshall L, Conner AC, Bill RM, Conner MT (2014) Human aquaporins: regulators of transcellular water flow. Biochim Biophys Acta 1840:1492–1506. https://doi.org/10.1016/j.bbagen.2013.09.033 · DOI
- de Grip WJ, Ganapathy S (2022) Rhodopsins: an excitingly versatile protein species for research, development and creative engineering. Front Chem 10:879609. https://doi.org/10.3389/fchem.2022.879609 · DOI
- Duan X, Nagel G, Gao S (2019) Mutated channelrhodopsins with increased sodium and calcium permeability. Applied Sciences 9:664. https://doi.org/10.3390/app9040664 · DOI
- Finn RN, Cerda J (2015) Evolution and functional diversity of aquaporins. Biol Bull 229:6–23. https://doi.org/10.1086/BBLv229n1p6 · DOI
- Govorunova EG, Gou Y, Sineshchekov OA, Li H, Lu X, Wang Y, Brown LS, St-Pierre F, Xue M, Spudich JL (2022) Kalium channelrhodopsins are natural light-gated potassium channels that mediate optogenetic inhibition. Nat Neurosci 25:967–974. https://doi.org/10.1038/s41593-022-01094-6 · DOI
- Govorunova EG, Sineshchekov OA, Brown LS, Bondar AN, Spudich JL (2022) Structural foundations of potassium selectivity in channelrhodopsins. mBio 13:e0303922. https://doi.org/10.1128/mbio.03039-22 · DOI
- Govorunova EG, Sineshchekov OA, Brown LS, Spudich JL (2022) Biophysical characterization of light-gated ion channels using planar automated patch clamp. Frontiers in Molecular Neuroscience 15:976910. https://doi.org/10.3389/fnmol.2022.976910 · DOI
- Govorunova EG, Sineshchekov OA, Janz R, Liu X, Spudich JL (2015) NEUROSCIENCE. Natural light-gated anion channels: a family of microbial rhodopsins for advanced optogenetics. Science 349:647–650. https://doi.org/10.1126/science.aaa7484 · DOI
- Hegemann P, Nagel G (2013) From channelrhodopsins to optogenetics. EMBO Mol Med 5:173–176. https://doi.org/10.1002/emmm.201202387 · DOI
- Jentsch TJ (2016) VRACs and other ion channels and transporters in the regulation of cell volume and beyond. Nat Rev Mol Cell Biol 17:293–307. https://doi.org/10.1038/nrm.2016.29 · DOI
- King LS, Kozono D, Agre P (2004) From structure to disease: the evolving tale of aquaporin biology. Nat Rev Mol Cell Biol 5:687–698. https://doi.org/10.1038/nrm1469 · DOI
- Leonard G, Labarre A, Milner DS, Monier A, Soanes D, Wideman JG, Maguire F, Stevens S, Sain D, Grau-Bove X, Sebe-Pedros A, Stajich JE, Paszkiewicz K, Brown MW, Hall N, Wickstead B, Richards TA (2018) Comparative genomic analysis of the ‘pseudofungus’ Hyphochytrium catenoides. Open Biol 8:170184. https://doi.org/10.1098/rsob.170184 · DOI
- Nagel G, Szellas T, Huhn W, Kateriya S, Adeishvili N, Berthold P, Ollig D, Hegemann P, Bamberg E (2003) Channelrhodopsin-2, a directly light-gated cation-selective membrane channel. Proc Natl Acad Sci U S A 100:13940–13945. https://doi.org/10.1073/pnas.1936192100 · DOI
- Omasits U, Ahrens CH, Muller S, Wollscheid B (2014) Protter: interactive protein feature visualization and integration with experimental proteomic data. Bioinformatics 30:884–886. https://doi.org/10.1093/bioinformatics/btt607 · DOI
- Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385–387. https://doi.org/10.1126/science.256.5055.385 · DOI
- Rojek A, Praetorius J, Frokiaer J, Nielsen S, Fenton RA (2008) A current view of the mammalian aquaglyceroporins. Annu Rev Physiol 70:301–327. https://doi.org/10.1146/annurev.physiol.70.113006.100452 · DOI
- Tamma G, Ranieri M, Di Mise A, Centrone M, Svelto M, Valenti G (2014) Glutathionylation of the aquaporin-2 water channel: a novel post-translational modification modulated by the oxidative stress. J Biol Chem 289:27807–27813. https://doi.org/10.1074/jbc.M114.586024 · DOI
- Tang R (2021) Optogenetic methods to regulate water transport and purify proteins. Doctoral thesis,. Universität Würzburg. https://doi.org/10.25972/OPUS-23173 · DOI
- Tradtrantip L, Jin BJ, Yao X, Anderson MO, Verkman AS (2017) Aquaporin-targeted therapeutics: State-of-the-Field. Adv Exp Med Biol 969:239–250. https://doi.org/10.1007/978-94-024-1057-0_16 · DOI
- Verkman AS, Anderson MO, Papadopoulos MC (2014) Aquaporins: important but elusive drug targets. Nat Rev Drug Discov 13:259–277. https://doi.org/10.1038/nrd4226 · DOI
- Weber W (1999) Ion currents of Xenopus laevis oocytes: state of the art. Biochim Biophys Acta 1421:213–233. https://doi.org/10.1016/s0005-2736(99)00135-2 · DOI
- Yukutake Y, Yasui M (2010) Regulation of water permeability through aquaporin-4. Neuroscience 168:885–891. https://doi.org/10.1016/j.neuroscience.2009.10.029 · DOI
- Zelenina M, Christensen BM, Palmer J, Nairn AC, Nielsen S, Aperia A (2000) Prostaglandin E(2) interaction with AVP: effects on AQP2 phosphorylation and distribution. Am J Physiol Renal Physiol 278:F388–F394. https://doi.org/10.1152/ajprenal.2000.278.3.F388 · DOI
- Zhou Y, Ding M, Gao S, Yu-Strzelczyk J, Krischke M, Duan X, Leide J, Riederer M, Mueller MJ, Hedrich R, Konrad KR, Nagel G (2021) Optogenetic control of plant growth by a microbial rhodopsin. Nat Plants 7:144–151. https://doi.org/10.1038/s41477-021-00853-w · DOI
Metadata
- Authors
- Lin, F., Tang, R., Zhang, C., Scholz, N., Nagel, G., & Gao, S.
- Affiliations
- University of Würzburg (DE)
- Fujian Medical University (CN)
- Leipzig University (DE)
- Corresponding author
- Gao, Shiqiang
- Venue
- Pflügers Archiv - European Journal of Physiology
- Published
- 2023-09-05
- Volume
- 475
- Issue
- 12
- Pages
- 1375-1385
- ISSN
- 0031-6768 (ISSN-L)
- 1432-2013
- PMC
- PMC10730689
- OpenAlex
- W4386456499
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 1 · 2023: 2
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Pflügers Archiv - European Journal of Physiology (publishedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Qucosa (Saxon State and University Library Dresden) (submittedVersion, cc-by)
- Funders
- Julius-Maximilians-Universität Würzburg
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Photoreceptor and optogenetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- aquaporins, water transport, optogenetics, osmotic gradient, water flux, Xenopus oocytes, light-gated ion channels
- MeSH terms
- Channelrhodopsins, Biological Transport, Oocytes, Permeability, Water, Aquaporins
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