...
  • 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 >The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors
【24h】

The Nck-interacting kinase phosphorylates ERM proteins for formation of lamellipodium by growth factors

机译：Nck相互作用激酶使ERM蛋白磷酸化，从而通过生长因子形成lalamlipodium

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 mammalian Ste20-like Nck-interacting kinase (NIK) and its orthologs Misshapen in Drosophila and Mig-15 in Caenorhabditis elegans have a conserved function in regulating cell morphology, although through poorly understood mechanisms. We report two previously unrecognized actions of NIK: regulation of lamellipodium formation by growth factors and phosphorylation of the ERM proteins ezrin, radixin, and moesin. ERM proteins regulate cell morphology and plasma membrane dynamics by reversibly anchoring actin filaments to integral plasma membrane proteins. In vitro assays show that NIK interacts directly with ERM proteins, binding their N termini and phosphorylating a conserved C-termi-nal threonine. In cells, NIK and phosphorylated ERM proteins localize at the distal margins of lamellipodia, and NIK activity is necessary for phosphorylation of ERM proteins induced by EGF and PDGF, but not by thrombin. Lamellipodium extension in response to growth factors is inhibited in cells expressing a kinase-inactive NIK, suppressed for NIK expression with siRNA oligonucleotides, or expressing ezrin T567A that cannot be phosphorylated. These data suggest that direct phosphorylation of ERM proteins by NIK constitutes a signaling mechanism controlling growth factor-induced membrane protrusion and cell morphology.
机译：哺乳动物的Ste20样Nck相互作用激酶（NIK）及其在果蝇中的直系同源物Misshapen和秀丽隐杆线虫的Mig-15在调节细胞形态方面具有保守的功能，尽管机制尚不清楚。我们报道了NIK的两个以前无法识别的作用：通过生长因子调节薄片状脂蛋白形成和ERM蛋白ezrin，Radixin和Moesin的磷酸化。 ERM蛋白通过将肌动蛋白丝可逆地锚定在完整的质膜蛋白上，从而调节细胞的形态和质膜动力学。体外测定表明，NIK与ERM蛋白直接相互作用，结合其N末端并磷酸化保守的C末端苏氨酸。在细胞中，NIK和磷酸化的ERM蛋白位于片状脂蛋白的远端边缘，而NIK活性对于EGF和PDGF而非凝血酶诱导的ERM蛋白的磷酸化是必需的。在表达无激酶活性的NIK，用siRNA寡核苷酸抑制NIK表达的细胞或表达无法磷酸化的ezrin T567A的细胞中，响应于生长因子的Lamellipodium延伸受到抑制。这些数据表明，NIK对ERM蛋白的直接磷酸化构成了控制生长因子诱导的膜突出和细胞形态的信号传导机制。

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