...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell cycle >Acm1 contributes to nuclear positioning by inhibiting Cdh1-substrate interactions
【24h】

Acm1 contributes to nuclear positioning by inhibiting Cdh1-substrate interactions

机译：Acm1通过抑制Cdh1-底物相互作用来促进核定位

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 anaphase-promoting complex (APC) is tightly regulated during cell division, often by pseudosubstrate binding to its coactivators Cdh1 and Cdc20. Budding yeast Acm1 is a Cdh1 pseudosubstrate inhibitor whose biological function is unknown. We show here that cells lacking Acm1 have defects in nuclear positioning and spindle morphology during mitosis. However, Cdh1 substrates are not destabilized in the absence of Acm1, and expression of inactive Cdh1 mutants that retain substrate binding is sufficient for the acm1 phenotype. We conclude that Acm1 is not required to inhibit APC Cdh1 activity, but rather prevents untimely Cdh1-substrate interactions. We further provide evidence suggesting that the substrate primarily responsible for the acm1 phenotype is the bud neck-localized kinase, Hsl1. Our results imply that at least some coactivator-substrate interactions require regulation. Several unrelated APC pseudosubstrates have been identified in diverse eukaryotes, and their ability to simultaneously inhibit enzymatic activity and substrate binding may partly explain why this regulatory mechanism has been selected repeatedly during evolution.
机译：后期促进复合物（APC）在细胞分裂过程中受到严格调节，通常是通过伪底物与其共激活物Cdh1和Cdc20结合而实现的。发芽酵母Acm1是一种Cdh1伪底物抑制剂，其生物学功能未知。我们在这里显示缺少Acm1的细胞在有丝分裂过程中在核定位和纺锤体形态上都有缺陷。但是，在没有Acm1的情况下Cdh1底物并不会不稳定，并且保留底物结合的无活性Cdh1突变体的表达对于acm1表型就足够了。我们得出的结论是，不需要Acm1来抑制APC Cdh1的活性，而是阻止了不合时宜的Cdh1-底物相互作用。我们进一步提供的证据表明，主要负责acm1表型的底物是芽颈定位的激酶Hsl1。我们的结果表明，至少某些共活化剂与底物的相互作用需要调节。在各种真核生物中已鉴定出几种无关的APC伪底物，它们同时抑制酶活性和底物结合的能力可能部分解释了为什么在进化过程中反复选择了这种调节机制的原因。

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