Endoplasmic reticulum export site formation and function in dendrites
Endoplasmic reticulum export site formation and function in dendrites
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DOI：
10.1523/jneurosci.4775-03.2004
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发表时间：
2004-04-14
影响因子：
5.3
通讯作者：
Fish, KN
中科院分区：
文献类型：
--
作者：
Aridor, M;Guzik, AK;Fish, KN
神经元的细长和极化特征使得受体靶向远端轴突和树突分支的质膜成为一项主要的分选任务。尽管大多数生物合成货物的合成、运输和分选被认为发生在体细胞中，但最近有报道称局部膜蛋白翻译和分选发生在树突和轴突中。我们研究了内质网（ER）输出发生在树突中的位置，使用体外渗透性神经元系统，使我们能够特异性地控制内质网输出位点的组装。我们发现，通过Sar1和COPII（外壳蛋白复合物II）的有序募集，内质网输出位点在整个树突树中有规律地组装。此外，代谢性谷氨酸受体的激活导致NMDA受体亚基NR1募集到重构的内质网输出位点。我们认为树突内质网对受体组装和输出的调节在调节受体表面表达和神经元功能中起着重要作用。
The elongated and polarized characteristics of neurons render targeting of receptors to the plasma membrane of distal axonal projections and dendritic branches a major sorting task. Although the majority of biosynthetic cargo synthesis, transport, and sorting are believed to occur in the soma, local membrane protein translation and sorting has been reported recently to take place in dendrites and axons. We investigated where endoplasmic reticulum (ER) export occurs in dendrites using an in vitro permeabilized neuron system that enables us to specifically control the assembly of ER export sites. We show that ER export sites are assembled regularly throughout the entire dendritic tree by the regulated sequential recruitment of Sar1 and COPII (coat protein complex II). Moreover, activation of metabotropic glutamate receptors leads to the recruitment of the NMDA receptor subunit NR1 to remodeled ER export sites. We propose that regulation of receptor assembly and export from the ER in dendrites plays an important role in modulating receptor surface expression and neuronal function.