The trafficking proteins Vacuolar Protein Sorting 35 and Neurobeachin interact with the glycine receptor β-subunit

被引：27
作者：
del Pino, Isabel [1 ]
Paarmann, Ingo [1 ]
Karas, Michael [2 ]
Kilimann, Manfred W. [3 ]
Betz, Heinrich [1 ]
机构：
[1] Max Planck Inst Brain Res, Dept Neurochem, D-60528 Frankfurt, Germany
[2] Goethe Univ Frankfurt, Inst Pharmaceut Chem, D-60438 Frankfurt, Germany
[3] Uppsala Univ, Dept Neurosci, S-75124 Uppsala, Sweden
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2011年 / 412卷 / 03期
关键词：
Glycine receptor; Spinal cord; Gephyrin; Neurobeachin; Retromer complex; Vacuolar Protein Sorting 35; CHEDIAK-HIGASHI-SYNDROME; SPLICE VARIANTS; GEPHYRIN; ACTIVATION; RETROMER; IDENTIFICATION; COMPLEXES; ENDOSOME; KINASE; VPS29;
D O I：
10.1016/j.bbrc.2011.07.110
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
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收藏
页码：435 / 440
页数：6
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