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首页> 外文期刊>Neuron >AMPA receptor tetramerization is mediated by q/r editing.
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AMPA receptor tetramerization is mediated by q/r editing.

机译:AMPA受体四聚体通过q / r编辑介导。

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摘要

AMPA-type glutamate receptors (AMPARs) play a major role in excitatory synaptic transmission and plasticity. Channel properties are largely dictated by their composition of the four subunits, GluR1-4 (or A-D). Here we show that AMPAR assembly and subunit stoichiometry are determined by RNA editing in the pore loop. We demonstrate that editing at the GluR2 Q/R site regulates AMPAR assembly at the step of tetramerization. Specifically, edited R subunits are largely unassembled and ER retained, whereas unedited Q subunits readily tetramerize and traffic to synapses. This assembly mechanism restricts the number of the functionally critical R subunits in AMPAR tetramers. Therefore, a single amino acid residue affects channel composition and, in turn, controls ion conduction through the majority of AMPARs in the brain.
机译:AMPA型谷氨酸受体(AMPAR)在兴奋性突触传递和可塑性中起主要作用。通道特性主要由其四个亚基GluR1-4(或A-D)的组成决定。在这里,我们显示AMPAR组装和亚基化学计量是由孔环中的RNA编辑决定的。我们证明,在GluR2 Q / R位点进行编辑可调节四聚化步骤中的AMPAR装配。具体而言,经编辑的R亚基在很大程度上未组装且保留了ER,而未经编辑的Q亚基易于四聚化并运输至突触。这种组装机制限制了AMPAR四聚体中功能关键的R亚基的数量。因此,单个氨基酸残基会影响通道组成,进而控制通过大脑中大多数AMPAR的离子传导。

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