• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>PLoS Clinical Trials >The Actin Binding Domain of βI-Spectrin Regulates the Morphological and Functional Dynamics of Dendritic Spines
【2h】

The Actin Binding Domain of βI-Spectrin Regulates the Morphological and Functional Dynamics of Dendritic Spines

机译：βI-Spectrin的肌动蛋白结合域调节树突棘的形态和功能动力学。

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Actin microfilaments regulate the size, shape and mobility of dendritic spines and are in turn regulated by actin binding proteins and small GTPases. The βI isoform of spectrin, a protein that links the actin cytoskeleton to membrane proteins, is present in spines. To understand its function, we expressed its actin-binding domain (ABD) in CA1 pyramidal neurons in hippocampal slice cultures. The ABD of βI-spectrin bundled actin in principal dendrites and was concentrated in dendritic spines, where it significantly increased the size of the spine head. These effects were not observed after expression of homologous ABDs of utrophin, dystrophin, and α-actinin. Treatment of slice cultures with latrunculin-B significantly decreased spine head size and decreased actin-GFP fluorescence in cells expressing the ABD of α-actinin, but not the ABD of βI-spectrin, suggesting that its presence inhibits actin depolymerization. We also observed an increase in the area of GFP-tagged PSD-95 in the spine head and an increase in the amplitude of mEPSCs at spines expressing the ABD of βI-spectrin. The effects of the βI-spectrin ABD on spine size and mEPSC amplitude were mimicked by expressing wild-type Rac3, a small GTPase that co-immunoprecipitates specifically with βI-spectrin in extracts of cultured cortical neurons. Spine size was normal in cells co-expressing a dominant negative Rac3 construct with the βI-spectrin ABD. We suggest that βI-spectrin is a synaptic protein that can modulate both the morphological and functional dynamics of dendritic spines, perhaps via interaction with actin and Rac3.
机译：肌动蛋白微丝调节树突棘的大小，形状和流动性，进而受肌动蛋白结合蛋白和小的GTPase调节。刺蛋白中存在血影蛋白的βI同工型，血肌蛋白是一种将肌动蛋白细胞骨架与膜蛋白连接的蛋白。为了解其功能，我们在海马切片培养物中的CA1锥体神经元中表达了其肌动蛋白结合域（ABD）。 βI-血影蛋白的ABD在主要树突中与肌动蛋白捆绑在一起，并集中在树突棘中，从而显着增加了脊柱头部的大小。表达了卵磷脂，肌营养不良蛋白和α-肌动蛋白的同源ABD后，未观察到这些作用。用latrunculin-B处理切片培养物可显着降低表达α-actininABD的细胞的脊柱头部大小，并降低actin-GFP荧光，但不能表达βI-spectrin的ABD，这表明其存在会抑制肌动蛋白解聚。我们还观察到在表达βI-血影蛋白ABD的脊柱中，带有GFP标记的PSD-95在脊柱头部的面积增加，而mEPSCs的幅度增加。通过表达野生型Rac3（一种小GTP酶，可与所培养的皮层神经元提取物特异地与βI-血影蛋白共免疫沉淀）模拟了βI-血影蛋白ABD对脊柱大小和mEPSC振幅的影响。在与βI-血影蛋白ABD共表达显性负性Rac3构建体的细胞中，脊柱大小正常。我们建议βI-spectrin是一种突触蛋白，可能通过与肌动蛋白和Rac3相互作用来调节树突棘的形态和功能动力学。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

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