• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell motility and the cytoskeleton >Src-dependent phosphorylation of Scar1 promotes its association with the Arp2/3 complex.
【24h】

Src-dependent phosphorylation of Scar1 promotes its association with the Arp2/3 complex.

机译：Scar1的Src依赖性磷酸化促进其与Arp2 / 3复合物的缔合。

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 WAVE/Scar proteins regulate actin polymerisation at the leading edge of motile cells via activation of the Arp2/3 complex in response to extracellular cues. Within cells they form part of a pentameric complex that is thought to regulate their ability to interact and activate the Arp2/3 complex. However, the exact mechanism for this is not known. We set out to assess whether phosphorylation of Scar1 by the non-receptor tyrosine kinase Src may influence the function of Scar1 and its ability to regulate Arp2/3-mediated actin polymerisation. We show that Scar1 is phosphorylated by Src in vitro and in vivo and identify tyrosine 125 as the major site in Scar1 to be phosphorylated in cells. Src-dependent phosphorylation of Scar1 on tyrosine 125 enhances its ability to bind to the Arp2/3 complex and regulates its ability to control actin polymerisation in cells. Thus, Src may act as an intermediary to regulate the activity of the Arp2/3 complex in response to external stimuli, via modulation of its interaction with WAVE/Scar proteins.
机译：WAVE / Scar蛋白通过响应细胞外信号而激活Arp2 / 3复合物，从而调节运动细胞前沿的肌动蛋白聚合。在细胞内，它们形成五聚体复合物的一部分，该五聚体复合物被认为调节其相互作用和激活Arp2 / 3复合物的能力。但是，确切的机制尚不清楚。我们着手评估非受体酪氨酸激酶Src对Scar1的磷酸化是否会影响Scar1的功能及其调节Arp2 / 3介导的肌动蛋白聚合的能力。我们显示Scar1在体外和体内被Src磷酸化，并鉴定酪氨酸125作为Scar1在细胞中被磷酸化的主要位点。 Scar1在酪氨酸125上的Src依赖性磷酸化增强了其与Arp2 / 3复合物结合的能力，并调节了其控制细胞中肌动蛋白聚合的能力。因此，Src可以通过调节其与WAVE / Scar蛋白的相互作用，充当调节Arp2 / 3复合物响应外部刺激的活性的中介。

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