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The Journal of Neuroscience, March 15, 2001, 21(6):1939-1948

Domain Interactions Regulating AMPA Receptor Desensitization

Kathryn M. Partin

Department of Anatomy and Neurobiology, Colorado State University, Fort Collins, Colorado 80523-1670

Desensitization is a common property of glutamate and other ligand-gated ion channels, yet its molecular mechanism is unknown. For glutamate receptors, agonist binding involves interactions with identified amino acids from two lobes and may result in stabilizing the lobes in a closed "clamshell" conformation. The present studies demonstrate that two structures, -strands 7 and 8 and -helices J and K, functionally interact with each other and likely form hinges between the two lobes, influencing the coupling between agonist binding and desensitization. Two amino acids identified within these regions form a solvent-exposed interface with a third amino acid, a mutation of which was shown previously to block receptor desensitization (L₅₀₇ in glutamate receptor 3). This interface may regulate a concerted conformational shift of the AMPA subtype of glutamate receptor subunits to the desensitized state.

Key words: AMPA receptors; glutamate receptors; cyclothiazide; desensitization; electrophysiology; ion channels; mutagenesis

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Copyright © 2001 Society for Neuroscience  0270-6474/01/2161939-10$05.00/0

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