...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The European Journal of Neuroscience >Role of the synprint site in presynaptic targeting of the calcium channel Ca(v)2.2 in hippocampal neurons.
【24h】

Role of the synprint site in presynaptic targeting of the calcium channel Ca(v)2.2 in hippocampal neurons.

机译：突触位点在海马神经元中钙通道Ca（v）2.2的突触前靶向中的作用。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Sequences in the cytoplasmic II-III loop of Ca(V)2 voltage-gated calcium channels, termed the synaptic protein interaction (synprint) site, are considered important for the functional incorporation of presynaptic calcium channels into the synaptic vesicle fusion apparatus. Two novel Ca(V)2.2 splice variants lack large parts of the cytoplasmic II-III loop (Delta1 R756-L1139, Delta2 K737-A1001) including the synprint protein-protein interaction domain. Here we expressed green fluorescent protein (GFP)-alpha(1B) subunit fusion constructs of Ca(V)2.2 splice variants in mouse hippocampal neurons to study their distribution in distinct neuronal compartments and to address the question of whether and how the synprint site functions in the presynaptic targeting of N-type calcium channels. Similar to full-length GFP-alpha(1B) but divergent from the somatodendritic alpha(1C)-HA (Ca(V)1.2) channel type, the splice variants GFP-alpha(1B)-Delta1 and GFP-alpha(1B)-Delta2 were targeted into the axons. Nevertheless, their ability to form bona fide presynaptic clusters was almost abolished for GFP-alpha(1B)-Delta1 and significantly reduced for GFP-alpha(1B)-Delta2. Thus, the synprint site is important for normal synaptic targeting of Ca(V)2.2 but not essential. Conversely, insertion of the synprint site into the II-III loop of alpha(1C)-HA did not restore axonal targeting or synaptic clustering. Together these results indicate that protein-protein interactions with the synprint site must cooperate with other targeting mechanisms in the incorporation of Ca(V)2.2 into presynaptic specializations of hippocampal neurons but are neither necessary nor sufficient for axonal targeting. The unique targeting properties of the splice variants lacking the synprint site are suggestive of specific functions of these calcium channels apart from activating fast synaptic transmission.
机译：Ca（V）2电压门控钙通道的细胞质II-I​​II回路中的序列，称为突触蛋白相互作用（突触）位点，被认为对于突触前钙通道功能整合到突触囊泡融合装置中很重要。两个新的Ca（V）2.2剪接变体缺少大部分的胞质II-I​​II环（Delta1 R756-L1139，Delta2 K737-A1001），包括synprint蛋白-蛋白相互作用域。在这里，我们在小鼠海马神经元中表达了Ca（V）2.2剪接变体的绿色荧光蛋白（GFP）-alpha（1B）亚基融合构建体，以研究它们在不同神经元区室中的分布，并解决了synprint位点是否起作用以及如何起作用的问题在突触前靶向N型钙通道。类似于全长GFP-alpha（1B），但与树突状alpha（1C）-HA（Ca（V）1.2）通道类型不同，剪接变体GFP-alpha（1B）-Delta1和GFP-alpha（1B） -Delta2被定位到轴突。但是，它们形成真正的突触前簇的能力几乎被GFP-alpha（1B）-Delta1废除，而对于GFP-alpha（1B）-Delta2则明显降低。因此，该突触位点对于正常的Ca（V）2.2突触目标很重要，但不是必需的。相反，将synprint网站插入到alpha（1C）-HA的II-III环中并不能恢复轴突靶向或突触聚类。这些结果在一起表明，蛋白质与蛋白质的相互作用与synprint位点必须配合其他靶向机制，将Ca（V）2.2整合到海马神经元的突触前专业中，但对于轴突靶向既不是必需的也不是足够的。缺乏突触位点的剪接变体的独特靶向特性表明这些钙通道的特定功能，除了激活快速突触传递。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号