...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural plasticity with preserved topology in the postsynaptic protein network
【24h】

Structural plasticity with preserved topology in the postsynaptic protein network

机译：突触后蛋白网络中保留拓扑结构的结构可塑性

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

The size, shape, and molecular arrangement of the postsynaptic density (PSD) determine the function of excitatory synapses in the brain. Here, we directly measured the internal dynamics of scaffold proteins within single living PSDs, focusing on the principal scaffold protein PSD-95. We found that individual PSDs undergo rapid, continuous changes in morphology driven by the actin cytoskeleton and regulated by synaptic activity. This structural plasticity is accompanied by rapid fluctuations in internal scaffold density over submicron distances. Using targeted photobleaching and photoactivation of PSD subregions, we show that PSD-95 is nearly immobile within the PSD, and PSD subdomains can be maintained over long periods. We propose a flexible matrix model of the PSD based on stable molecular positioning of PSD-95 scaffolds.
机译：突触后密度（PSD）的大小，形状和分子排列决定了大脑中兴奋性突触的功能。在这里，我们直接测量了单个活动PSD内支架蛋白的内部动力学，重点研究了主要支架蛋白PSD-95。我们发现，单个PSD受到肌动蛋白细胞骨架驱动并受突触活性调节的形态快速，连续变化。这种结构可塑性伴随着内部支架密度在亚微米距离上的快速波动。使用靶向光漂白和PSD子区域的光活化，我们显示PSD-95在PSD内几乎是不动的，并且PSD子域可以长期维持。我们基于PSD-95支架的稳定分子定位，提出了PSD的灵活矩阵模型。

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