• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >Regulation of Microtubule Assembly by Tau and not by Pin1
【24h】

Regulation of Microtubule Assembly by Tau and not by Pin1

机译：Tau而非Pin1对微管组装的监管

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 molecular mechanism by which the microtubule-associated protein (MAP) tau regulates the formation of microtubules (MTs) is poorly understood. The activity of tau is controlled via phosphorylation at specific Ser/Thr sites. Of those phosphorylation sites, 17 precede a proline, making them potential recognition sites for the peptidyl-prolyl isomerase Pin1. Pin1 binding and catalysis of phosphorylated tau at the AT180 epitope, which was implicated in Alzheimer's disease, has been reported to be crucial for restoring tau's ability to promote MT polymerization in vitro and in vivo [1]. Surprisingly, we discover that Pin1 does not promote phosphorylated tau-induced MT formation in vitro, refuting the commonly accepted model in which Pin1 binding and catalysis on the A180 epitope restores the function of the Alzheimer's associated phosphorylated tau in tubulin assembly [1, 2].
机译：对微管相关蛋白（MAP）tau调节微管（MTs）形成的分子机理了解甚少。 tau的活性通过特定Ser / Thr位点的磷酸化来控制。在那些磷酸化位点中，有17个位于脯氨酸之前，使它们成为肽基-脯氨酰异构酶Pin1的潜在识别位点。据报道，AT1表位的Pin1结合和磷酸化tau的催化作用与阿尔茨海默氏病有关，对于恢复tau在体外和体内促进MT聚合的能力至关重要。出乎意料的是，我们发现Pin1不会在体外促进tau诱导的磷酸化MT的形成，驳斥了普遍接受的模型，其中Pin1对A180表位的结合和催化可恢复阿尔茨海默氏症相关的磷酸化tau在微管蛋白装配中的功能[1、2] 。

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