...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >The Scaffold Protein PDZK1 Undergoes a Head-to-Tail Intramolecular Association That Negatively Regulates Its Interaction with EBP50
【24h】

The Scaffold Protein PDZK1 Undergoes a Head-to-Tail Intramolecular Association That Negatively Regulates Its Interaction with EBP50

机译：支架蛋白PDZK1经历了从头到尾的分子内缔合，其负调节其与EBP50的相互作用。

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

PDZK1 (also known as CAP70, NHERF3, or NaPi-Cap1) is a scaffolding protein composednof four PDZ (Post-Synaptic Density-95, Discs Large, Zonula Occludens-1) domains followed by a shortncarboxyl-terminal tail. This scaffold acts as a mediator of localization and expression levels of multiplenreceptors in the kidney, liver, and endothelium. Here, we characterize the self-association properties ofnthe protein. PDZK1 can undergo modest homodimerization in vivo and in vitro through self-associationninvolving its third PDZ domain. In addition, the tail of PDZK1 interacts in an intramolecular fashion withnthe first PDZ domain, but this interaction does not contribute to dimer formation. The interaction betweennthe tail of PDZK1 and its first PDZ domain induces the protein to adopt a more compact conformation.nA head-to-tail association has also been reported for EBP50/NHERF1, a two-PDZ domain member of thensame scaffolding protein family as PDZK1, and shown to regulate binding of target proteins to the EBP50nPDZ domains. As opposed to EBP50, the association of PDZK1 with specific ligands for its PDZ domainsnis unaffected by the intramolecular association, establishing a different mode of interaction among thesentwo members of the same scaffolding family. However, the tail of PDZK1 interacts with the PDZ domainsnof EBP50, and this interaction is negatively regulated by the intramolecular association of PDZK1. Thus,nwe have uncovered a regulated association between the two PDZ-containing scaffolding molecules, PDZK1nand EBP50.
机译：PDZK1（也称为CAP70，NHERF3或NaPi-Cap1）是一种支架蛋白，由四个PDZ（突触后密度95，大圆盘，Zonula Occludens-1）域和一个短羧基末端尾巴组成。该支架充当肾脏，肝脏和内皮中多受体的定位和表达水平的介质。在这里，我们表征蛋白质的自缔合特性。 PDZK1可以通过涉及其第三个PDZ域的自缔合在体内和体外进行适度的二聚化。另外，PDZK1的尾部以分子内的方式与第一个PDZ结构域相互作用，但是这种相互作用对二聚体的形成没有贡献。 PDZK1尾部与其第一个PDZ结构域之间的相互作用诱导该蛋白采用更紧密的构象。也有报道说EBP50 / NHERF1的头尾相关性，这是与PDZK1相同支架蛋白家族的两个PDZ结构域成员。 ，并显示可调节靶蛋白与EBP50nPDZ域的结合。与EBP50相反，PDZK1与其PDZ结构域的特异性配体的结合不受分子内结合的影响，从而在同一支架家族的两个成员之间建立了不同的相互作用方式。然而，PDZK1的尾巴与EBP50的PDZ域相互作用，并且这种相互作用受到PDZK1分子内缔合的负调控。因此，我们已经发现了两个含PDZ的支架分子PDZK1n和EBP50之间的调控联系。

著录项

  • 来源
    《Biochemistry》 |2009年第10期|p.2261-2271|共11页
  • 作者

    David P. LaLonde and Anthony Bretscher;

  • 作者单位

    Weill Institute for Cell and Molecular Biology, Department of Molecular Biology and Genetics, Cornell UniVersity,Ithaca, New York 14853;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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