Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor
Proteomic analysis revealed a novel synaptic proline-rich membrane protein (PRR7) associated with PSD-95 and NMDA receptor
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DOI：
10.1016/j.bbrc.2004.11.154
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发表时间：
2005-02-04
影响因子：
3.1
通讯作者：
Fujiyoshi, Y
中科院分区：
文献类型：
--
作者：
Murata, Y;Doi, T;Fujiyoshi, Y
蛋白质组学分析揭示了一种新的突触脯氨酸丰富的膜蛋白：PRR 7（脯氨酸丰富7），在突触后密度（PSD）的部分大鼠前脑。PRR 7是269个氨基酸残基长，并且显示出独特的结构，其由非常短的N-末端胞外区、单个跨膜结构域和具有富含脯氨酸的序列和C-末端1型PDZ结合基序的胞质结构域组成。PRR 7的一部分随着突触成熟沿着积累在棘中，并且在大鼠海马神经培养物中以点状模式与PSD-95共定位。免疫沉淀和GST下拉分析表明，PRR 7结合PSD-95的第三PDZ结构域。此外，NMDA受体亚基NR 1和NR 2B与PRR 7特异性共免疫沉淀。这些结果表明PRR 7通过与NMDA受体和PSD-95的相互作用以及PSD核心形成参与调节神经活动。(C)2004年爱思唯尔公司All rights reserved.
Proteomic analyses have revealed a novel synaptic proline-rich membrane protein: PRR7 (proline rich 7), in the postsynaptic density (PSD) fraction of rat forebrain. PRR7 is 269 amino acid residues long, and displays a unique architecture, composed of a very short N-terminal extracellular region, a single membrane spanning domain, and a cytoplasmic domain possessing a proline-rich sequence and a C-terminal type-1 PDZ binding motif. A fraction of PRR7 accumulates in spines along with synapse maturation, and colocalizes with PSD-95 in a punctate pattern in rat hippocampal neural cultures. Immunoprecipitation and GST pull-down assays demonstrated that PRR7 binds to the third PDZ domain of PSD-95. In addition, the NMDA receptor subunits, NR1 and NR2B, specifically co-immunoprecipitated with PRR7. These results suggest that PRR7 is involved in modulating neural activities via interactions with the NMDA receptor and PSD-95, and PSD core formation. (C) 2004 Elsevier Inc. All rights reserved.