Developmentally Regulated, Combinatorial RNA Processing Modulates AMPA Receptor Biogenesis

Abstract

(Neuron 51, 85–97; July 6, 2006) At the time of publication of our work, we did not provide access to the coordinates for the crystal structure of the R/G unedited form of the GluR2-flip ligand binding domain. We apologize for this oversight. This information is now freely available at the Protein Data Bank (www.pdb.org) under accession number 2uxa. Developmentally Regulated, Combinatorial RNA Processing Modulates AMPA Receptor BiogenesisGreger et al.NeuronJuly 06, 2006In BriefThe subunit composition determines AMPA receptor (AMPA-R) function and trafficking. Mechanisms underlying channel assembly are thus central to the efficacy and plasticity of glutamatergic synapses. We previously showed that RNA editing at the Q/R site of the GluR2 subunit contributes to the assembly of AMPA-R heteromers by attenuating formation of GluR2 homotetramers. Here we report that this function of the Q/R site depends on subunit contacts between adjacent ligand binding domains (LBDs). Changes of LBD interface contacts alter GluR2 assembly properties, forward traffic, and expression at synapses. Full-Text PDF Open Archive