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• W2973956888 abstract "Abstract Desensitization is a canonical property of ligand-gated ion channels, causing progressive current decline in the continued presence of agonist. AMPA-type glutamate receptors (AMPARs), which mediate fast excitatory signaling throughout the brain, exhibit profound desensitization. Recent cryo-EM studies of AMPAR assemblies show their ion channels to be closed in the desensitized state. Here we present evidence that homomeric Q/R-edited AMPARs still allow ions to flow when the receptors are desensitized. GluA2(R) expressed alone, or with auxiliary subunits (γ-2, γ-8 or GSG1L), generates large fractional steady-state currents and anomalous current-variance relationships. Our results from fluctuation analysis, single-channel recording, and kinetic modeling, suggest that the steady-state current is mediated predominantly by conducting desensitized receptors. When combined with crystallography this unique functional readout of a hitherto silent state enabled us to examine cross-linked cysteine mutants to probe the conformation of the desensitized ligand binding domain of functioning AMPAR complexes." @default.
• W2973956888 created "2019-09-26" @default.
• W2973956888 creator A5023645727 @default.
• W2973956888 creator A5034351921 @default.
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• W2973956888 creator A5069305015 @default.
• W2973956888 creator A5071371736 @default.
• W2973956888 creator A5076267142 @default.
• W2973956888 date "2019-09-20" @default.
• W2973956888 modified "2023-10-16" @default.
• W2973956888 title "Homomeric GluA2(R) AMPA receptors can conduct when desensitized" @default.
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• W2973956888 doi "https://doi.org/10.1038/s41467-019-12280-9" @default.
• W2973956888 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6754398" @default.
• W2973956888 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31541113" @default.
• W2973956888 hasPublicationYear "2019" @default.
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