A tetrameric subunit stoichiometry for a glutamate receptor-channel complex

Neuroreport. 1998 Jan 26;9(2):327-31. doi: 10.1097/00001756-199801260-00027.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Excitatory Amino Acid Agonists / pharmacology
  • Ion Channels / chemistry*
  • Ion Channels / genetics
  • Kainic Acid / pharmacology
  • Mutagenesis, Site-Directed
  • Mutation
  • Oocytes / metabolism
  • Quisqualic Acid / pharmacology
  • RNA, Messenger / biosynthesis
  • Receptors, AMPA / chemistry
  • Receptors, AMPA / genetics
  • Receptors, Glutamate / chemistry*
  • Receptors, Glutamate / genetics
  • Xenopus

Substances

  • Excitatory Amino Acid Agonists
  • Ion Channels
  • RNA, Messenger
  • Receptors, AMPA
  • Receptors, Glutamate
  • Quisqualic Acid
  • Kainic Acid