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- W4308784150 abstract "Abstract Pentameric ligand-gated ion channels represent a large family of receptors comprising an extracellular domain, four transmembrane helices and a cytosolic intracellular domain (ICD). ICDs play important roles in receptor localization and trafficking, thus regulating synaptic activity and plasticity. Glycine and GABA type A receptor ICDs bind to the scaffolding protein gephyrin, a master regulator of inhibitory synapses. Here we report the use of yeast lumazine synthase as soluble pentameric protein scaffold for the study of receptor ICDs derived from GlyR α1− and β-subunits. We were able to create ICDs assemblies in a homo- (LS-βICD) and hetero-pentameric state (LS-αβICD) and provide first-in-class structural insights on their high structural flexibility using small angle X-ray scattering. We report a high-affinity interaction between the LS-αβICD and gephyrin leading to the in vitro formation of high-molecular mega-Dalton complexes composed of three gephyrin trimers and three pentamers as basic building block. Depending on the stoichiometric ratios between gephyrin and LS-ICDs the formed complexes grow or shrink in size. In cells, LS-ICDs efficiently recruited gephyrin and were able to accumulate gephyrin at GABAergic synapses in neurons. Our findings collectively propose a new, potentially general, mechanistic concept for a gephyrin-dependent bridging of GlyRs at the inhibitory synapse." @default.
- W4308784150 created "2022-11-15" @default.
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- W4308784150 date "2022-11-11" @default.
- W4308784150 modified "2023-09-26" @default.
- W4308784150 title "Pentameric assembly of glycine receptor intracellular domains provides insights into gephyrin clustering" @default.
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- W4308784150 doi "https://doi.org/10.1101/2022.11.10.512828" @default.
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