The Tetrameric Structure of a Glutamate Receptor Channel

• Published in: Science (American Association for the Advancement of Science) 1998-06, Vol.280 (5369), p.1596-1599
• Main Authors: Rosenmund, Christian, Stern-Bach, Yael, Stevens, Charles F.
• Format: Article
• Language: English
• Subjects: Agonists; Aminoacid receptors (glycine, glutamate, gaba); Binding Sites; Biological and medical sciences; Brain; Cell Line; Cell receptors; Cell structures and functions; Chemistry; Desensitization; Electric Conductivity; Excitatory Amino Acid Agonists - metabolism; Excitatory Amino Acid Antagonists - metabolism; Fundamental and applied biological sciences. Psychology; GluK2 Kainate Receptor; Glutamate; Glutamate receptors; Histograms; Humans; Ligands; Macromolecular Substances; Modeling; Models, Biological; Molecular and cellular biology; Neurons; Neuroscience; Observation; Patch-Clamp Techniques; Quinoxalines - metabolism; Quisqualic acid; Quisqualic Acid - metabolism; Receptors; Receptors, AMPA - agonists; Receptors, AMPA - antagonists & inhibitors; Receptors, AMPA - chemistry; Receptors, AMPA - metabolism; Receptors, Glutamate - chemistry; Receptors, Glutamate - metabolism; Receptors, Kainic Acid - agonists; Receptors, Kainic Acid - antagonists & inhibitors; Receptors, Kainic Acid - chemistry; Receptors, Kainic Acid - metabolism; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Staircases
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.280.5369.1596

The subunit stoichiometry of several ligand-gated ion Channel receptors is still unknown. A Counting method was developed to determine the number of subunits in one family of brain glutamate receptors. Successful application of this method in an HEK cell line provides evidence that ionotropic glutamate receptors share a tetrameric structure with the voltage-gated potassium channels. The average conductance of these channels depends on how many subunits are occupied by an agonist.