2uxa
CRYSTAL STRUCTURE OF THE GLUR2-FLIP LIGAND BINDING DOMAIN, R/G UNEDITED.
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OverviewOverview
The 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. Interestingly, developmentally regulated RNA editing within the LBD (at the R/G site) produces analogous effects. Our data reveal that editing to glycine reduces the self-assembly competence of this critical subunit and slows GluR2 maturation in the endoplasmic reticulum (ER). Therefore, RNA editing sites, located at strategic subunit interfaces, shape AMPA-R assembly and trafficking in a developmentally regulated manner.
About this StructureAbout this Structure
2UXA is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Developmentally regulated, combinatorial RNA processing modulates AMPA receptor biogenesis., Greger IH, Akamine P, Khatri L, Ziff EB, Neuron. 2006 Jul 6;51(1):85-97. PMID:16815334
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