The trafficking proteins Vacuolar Protein Sorting 35 and Neurobeachin interact with the glycine receptor β-subunit
The trafficking proteins Vacuolar Protein Sorting 35 and Neurobeachin interact with the glycine receptor β-subunit
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DOI：
10.1016/j.bbrc.2011.07.110
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发表时间：
2011-09-02
影响因子：
3.1
通讯作者：
Betz, Heinrich
中科院分区：
文献类型：
--
作者：
del Pino, Isabel;Paarmann, Ingo;Betz, Heinrich
抑制性甘氨酸受体（GlyR）由于其β-亚基与支架蛋白桥蛋白的高亲和力相互作用而密集地堆积在突触后膜中。在这里，我们使用了一种基于亲和力的蛋白质组学方法，以确定运输蛋白的蛋白质分子蛋白分选35（Vps 35）和神经海滩蛋白（Nbea）作为新的GlyR β亚基（GlyR β）相互作用的蛋白质在大鼠大脑。重组Vps 35和Nbea的中心片段结合到谷胱甘肽-S-转移酶下拉中GlyR β的大细胞内环;此外，Vps 35显示结合桥蛋白。脊髓切片的免疫细胞化学染色显示Nbea免疫反应性并列和共定位与抑制性突触的标记蛋白。我们的数据与Vps 35和Nbea在突触GlyRs和可能的其他神经递质受体的检索和高尔基体后贩运中的作用一致。(C)2011 Elsevier Inc. All rights reserved.
Inhibitory glycine receptors (GlyRs) are densely packed in the postsynaptic membrane due to a high-affinity interaction of their beta-subunits with the scaffolding protein gephyrin. Here, we used an affinity-based proteomic approach to identify the trafficking proteins Vacuolar Protein Sorting 35 (Vps35) and Neurobeachin (Nbea) as novel GlyR beta-subunit (GlyR beta) interacting proteins in rat brain. Recombinant Vps35 and a central fragment of Nbea bound to the large intracellular loop of GlyR beta in glutathione-S-transferase pull-downs; in addition, Vps35 displayed binding to gephyrin. Immunocytochemical staining of spinal cord sections revealed Nbea immunoreactivity apposed to and colocalizing with marker proteins of inhibitory synapses. Our data are consistent with roles of Vps35 and Nbea in the retrieval and post-Golgi trafficking of synaptic GlyRs and possibly other neurotransmitter receptors. (C) 2011 Elsevier Inc. All rights reserved.