A tetrameric subunit stoichiometry for a glutamate receptor-channel complex.
The structure of glutamate receptor-channel (GluR) subunits has recently been shown to differ from that of other ligand-gated channels and to contain a voltage-gated channel-like pore-forming motif. The view that the structure of GluR complexes is similar to the pentameric structure of other ligand-gated channels was questioned here. Studies of the response properties of the GluR1 subunit of the AMPA subtype of GluRs, co-expressed in Xenopus oocytes with its L646A mutant, which differs only by a greatly reduced sensitivity to quisqualate, provide new evidence suggesting that the GluR1 homomeric receptor channel has a tetrameric structure.
Mano
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Department of Neurobiology, Weizmann Institute of Science, Rehovot, Israel.
Teichberg
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D000818:Animals; D018690:Excitatory Amino Acid Agonists / Q000494:pharmacology; D007473:Ion Channels / Q000737:chemistry* / Q000235:genetics; D007608:Kainic Acid / Q000494:pharmacology; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D009865:Oocytes / Q000378:metabolism; D016318:Quisqualic Acid / Q000494:pharmacology; D012333:RNA, Messenger / Q000096:biosynthesis; D018091:Receptors, AMPA / Q000737:chemistry / Q000235:genetics; D017470:Receptors, Glutamate / Q000737:chemistry* / Q000235:genetics; D014981:Xenopus
D018690:Excitatory Amino Acid Agonists; D007473:Ion Channels; D012333:RNA, Messenger; D018091:Receptors, AMPA; D017470:Receptors, Glutamate; D016318:Quisqualic Acid; D007608:Kainic Acid