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- W1992806875 abstract "Several mechanistic aspects of ligand-gated ion channels remain poorly understood, such as the allosteric coupling between different subunits. The development of photoswitchable ligands that can be covalently attached to specifically introduced cysteine residues [1, 2] enables us to overcome some limitations of conventional studies. Using a glutamate analogue combined with an azobenzene photoswitch, we can study activation, deactivation and desensitization of ionotropic glutamate receptors (iGluRs). With this approach, ligand binding and unbinding can be precisely controlled using short light pulses, and are not limited by the time required to apply and remove the ligand. Furthermore, ligand binding can be restricted to a specific subset of the four subunits constituting the tetrameric channel. Here we used voltage-clamp recordings to measure the time courses of channel opening and closing upon full and partial activation with short pulses of light. Even low light doses lead to opening of iGluR6 on the submillisecond timescale followed by rapid desensitization. Extending the photoswitching experiments to single channel recordings and complexes with defined subunit stochiometries will provide further information on how single subunits contribute to the function of this important class of signaling molecules. 1. Volgraf M. et al., Nat. Chem. Biol. (2006) 2: 47. 2. Gorostiza P. et al., Proc. Natl. Acad. Sci. USA (2007) 104: 10865. This work was supported by a Deutsche Forschungsgemeinschaft fellowship to A. Reiner and the NIH Nanomedicine Development Center for the Optical Control of Biological Function (5PN2EY018241)." @default.
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- W1992806875 date "2011-02-01" @default.
- W1992806875 modified "2023-10-18" @default.
- W1992806875 title "Mechanistic Studies on Ionotropic Glutamate Receptors Using Tethered Photoswitchable Ligands" @default.
- W1992806875 doi "https://doi.org/10.1016/j.bpj.2010.12.1677" @default.
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