AMPA Receptor Tetramerization Is Mediated by Q/R Editing

  title={AMPA Receptor Tetramerization Is Mediated by Q/R Editing},
  author={Ingo H. Greger and Latika Khatri and Xiangpeng Kong and Edward Benjamin Ziff},

Figures and Tables from this paper

Sculpting AMPA receptor formation and function by alternative RNA processing
Recoded sites line interfaces of subunit polypeptides are ideally positioned to modulate receptor assembly and the genomic arrangement of the R/G editing site within the splice donor of the alternative flip/flop exons may facilitate a cross-talk between these elements.
Assembly and Stoichiometry of the AMPA Receptor and Transmembrane AMPA Receptor Regulatory Protein Complex
A novel strategy to determine the assembly and stoichiometry of the AMPA receptor and TARP complex was developed and it was found that functional AMPA receptors indeed assembled as a tetramer in a dimer-of-dimers structure.
AMPA receptor assembly: atomic determinants and built-in modulators.
The role of alternative RNA processing in the ligand-binding domain, which modulates a central subunit interface and has the capacity to modulate receptor formation in response to external cues, is discussed.
Q/R Site Editing Controls Kainate Receptor Inhibition by Membrane Fatty Acids
It is shown that fatty acid blockade of recombinant homomeric and heteromeric kainate receptors is strongly dependent on editing at the Q/R site, and Recombinant channels that include unedited subunits exhibit significantly weaker block than channels made up of fully edited subunits.
The Biochemistry, Ultrastructure, and Subunit Assembly Mechanism of AMPA Receptors
  • T. Nakagawa
  • Biology, Chemistry
    Molecular Neurobiology
  • 2010
The current ultrastructural data on the receptors and the receptor-expressing stable cell lines that were developed during the course of these studies are useful resources for high throughput drug screening and further drug designing and are getting closer to understanding the precise mechanisms of AMPA-R-mediated synaptic plasticity.
GluA1 signal peptide determines the spatial assembly of heteromeric AMPA receptors
The spatial assembly of an important type of glutamate receptors in the brain is uncovered and a novel function of signal peptides is revealed and is controlled by the excisable signal peptide sequences.
AMPA receptors in the synapse turnover by monomer diffusion
It is demonstrated that AMPAR tetramers are not stable entities and readily fall apart to dimers and monomers that could reform to tetramer at the synapse, and that rapidly diffusing monomers in the plasma membrane are primarily responsible for the AMPAR turnover in the synapses.


RNA Editing at Arg607 Controls AMPA Receptor Exit from the Endoplasmic Reticulum
Single-Channel Properties of Recombinant AMPA Receptors Depend on RNA Editing, Splice Variation, and Subunit Composition
It is suggested that the single-channel conductance of certain recombinant AMPA receptors may be determined by the expression of edited GluR2 subunits in neurons.
A tetrameric subunit stoichiometry for a glutamate receptor–channel complex
Study of the response properties of the GluR1 subunit of the AMPA subtype of GluRs, co-expressin Xenopus oocytes with its L646A mutant, provide new evidence suggesting that the GLUR1 homomeric receptor channel has a tetrameric structure.
Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction.
Results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.
Synaptic activity at calcium-permeable AMPA receptors induces a switch in receptor subtype
A new form of synaptic plasticity is described—a rapid and lasting change in the subunit composition and Ca2+ permeability of AMPARs at cerebellar stellate cell synapses following synaptic activity.
Dimensions and ion selectivity of recombinant AMPA and kainate receptor channels and their dependence on Q/R site residues.
The results indicated that the diameters of the narrow portion of AMPAR and KAR channels of different subunit composition and of widely different ion selectivity are comparable and the differences in the anion versus cation selectivity, in Ca2+ permeability and in channel conductance are likely to be determined by the difference in charge density of the channel.