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- W2912200569 abstract "Pentameric ligand-gated ion channels (pLGICs) are membrane receptors found in both prokaryotes, like GLIC, and eukaryotes. Amongst them, Glycine Receptors (GlyR), GABAA receptors or nicotinic receptors are responsible for fast synaptic transmission in the mammalian brain and are modulated by several classes of molecules of therapeutic interest. Congenital mutations on these proteins can cause severe pathologies such as epilepsy and startle disease. Structural and functional properties of this family of receptors are widely studied and we aim to integrate these two aspects by investigating the dynamics of structural changes of GLIC and GlyR during activation. To do so, we grafted small fluorescent dyes on the protein at different positions by reaction on engineered cysteines. The change in distance with surrounding tryptophans causes changes in fluorescence intensities (quenching) and enables a detailed characterization of conformational reorganizations. We performed a thorough analysis of modulators and mutations affecting GLIC function, giving insights into the coupling mechanisms between extracellular and transmembrane domains. For the study of human GlyR, we developed a voltage clamp fluorometry set-up which enables the concomitant recording of current by electrophysiology and fluorescence to apply the tryptophan quenching method. Specific pairs allow to study allosteric mechanisms of extracellular and transmembrane domains coupling and to understand their perturbation by modulators and mutations inducing startle disease. Overall, this work will contribute to a better understanding of allosteric mechanisms governing pLGICs activity and bring about new strategies to find novel allosteric modulators with potential as therapeutic drugs." @default.
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- W2912200569 date "2019-02-01" @default.
- W2912200569 modified "2023-09-25" @default.
- W2912200569 title "Allosteric Transitions of Pentameric Ligand-Gated Ion Channels Studied by Fluorescence Quenching to Explore Pathological Mutations and Pharmacological Effectors" @default.
- W2912200569 doi "https://doi.org/10.1016/j.bpj.2018.11.2141" @default.
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