Plasma membrane insertion of the AMPA receptor GluA2 subunit is regulated by NSF binding and Q/R editing of the ion pore
Plasma membrane insertion of the AMPA receptor GluA2 subunit is regulated by NSF binding and Q/R editing of the ion pore
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DOI：
10.1073/pnas.1006584107
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发表时间：
2010-06-15
影响因子：
11.1
通讯作者：
Huganir, Richard L.
中科院分区：
文献类型：
--
作者：
Araki, Yoichi;Lin, Da-Ting;Huganir, Richard L.
AMPA受体向质膜的传递是这些受体的突触传递和突触传递调节的关键步骤。为了直接可视化含有AMPA受体GluA 2亚基的运输囊泡与质膜的融合事件，我们使用pHluorin标记的GluA 2亚基和全内反射荧光显微镜。我们表明，质膜插入的GluA 2需要在其细胞内的胞质结构域的NSF结合位点和RNA编辑的离子通道区域中的Q/R位点在GluA 2质膜插入中起着关键作用。最后，我们表明，异聚体GluA 2/3受体的质膜插入遵循相同的规则，同聚体GluA 2受体。这些结果表明，含有AMPA受体的GluA 2的质膜递送受其独特的结构元件调节。
The delivery of AMPA receptors to the plasma membrane is a critical step both for the synaptic delivery of these receptors and for the regulation of synaptic transmission. To directly visualize fusion events of transport vesicles containing the AMPA receptor GluA2 subunit with the plasma membrane we used pHluorin-tagged GluA2 subunits and total internal reflection fluorescence microscopy. We demonstrate that the plasma membrane insertion of GluA2 requires the NSF binding site within its intracellular cytoplasmic domain and that RNA editing of the Q/R site in the ion channel region plays a key role in GluA2 plasma membrane insertion. Finally, we show that plasma membrane insertion of heteromeric GluA2/3 receptors follows the same rules as homomeric GluA2 receptors. These results demonstrate that the plasma membrane delivery of GluA2 containing AMPA receptors is regulated by its unique structural elements.