...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Structure >An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B
【24h】

An Atypical MAGUK GK Target Recognition Mode Revealed by the Interaction between DLG and KIF13B

机译：DLG与KIF13B相互作用揭示非典型MAGUK GK目标识别模式

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 membrane-associated guanylate kinase (MAGUK) scaffold proteins share a signature guanylate kinase (GK) domain. Despite their diverse functional roles in cell polarity control and synaptic signaling, the currently known mode of action of MAGUK GK is via its binding to phosphorylated short peptides from target proteins. Here, we discover that the GK domain of DLG MAGUK binds to an unphosphorylated and autonomously folded domain within the stalk region (MAGUK binding stalk [MBS] domain) of a kinesin motor KIF13B with high specificity and affinity. The structure of DLG4 GK in complex with KIF13B MBS reveals the molecular mechanism governing this atypical GK/target recognition mode and provides insights into DLG/KIF13B complex-mediated regulation of diverse cellular processes such as asymmetric cell division. We further show that binding to non-phosphorylated targets is another general property of MAGUK GKs, thus expanding the mechanisms of action of the MAGUK family proteins.
机译：膜相关的鸟苷酸激酶（MAGUK）支架蛋白共享一个标志性鸟苷酸激酶（GK）域。尽管它们在细胞极性控制和突触信号传导中具有多种功能，但MAGUK GK的当前已知作用方式是通过其与靶蛋白的磷酸化短肽结合而实现的。在这里，我们发现DLG MAGUK的GK结构域以高特异性和亲和力与驱动蛋白马达KIF13B的茎区域（MAGUK结合茎[MBS]域）内的未磷酸化和自主折叠的域结合。与KIF13B MBS结合的DLG4 GK的结构揭示了控制这种非典型GK /靶标识别模式的分子机制，并为DLG / KIF13B复杂介导的多种细胞过程（例如不对称细胞分裂）的调控提供了见识。我们进一步表明，与非磷酸化靶标结合是MAGUK GK的另一个一般特性，从而扩展了MAGUK家族蛋白的作用机理。

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