...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >The Mitogen-Activated Protein Kinase Slt2 Regulates Nuclear Retention of Non-Heat Shock mRNAs during Heat Shock-Induced Stress
【24h】

The Mitogen-Activated Protein Kinase Slt2 Regulates Nuclear Retention of Non-Heat Shock mRNAs during Heat Shock-Induced Stress

机译：丝裂原激活的蛋白激酶Slt2调节热休克诱导的应激过程中非热休克mRNA的核保留。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Cellular adaptation to environmental stress conditions requires rapid and specific changes in gene expression. During heat shock, most polyadenylated mRNAs are retained in the nucleus, whereas the export of heat shock-induced mRNAs is allowed. Although essential mRNA export factors are known, the precise mechanism for regulating transport is not fully understood. Here we find that during heat shock in Saccharomyces cerevisiae, the mRNA-binding protein Nab2 is phosphorylated on threonine 178 and serine 180 by the mitogen-activated protein (MAP) kinase Slt2/Mpk1. Slt2 is required for nuclear poly(A+) mRNA accumulation upon heat shock, and thermotolerance is decreased in a nup42 nab2-T178A/S180A mutant. Coincident with phosphorylation, Nab2 and Yra1 colocalize in nuclear foci with Mlp1, a protein involved in mRNA retention. Nab2 nuclear focus formation and Nab2 phosphorylation are independent, suggesting that heat shock induces multiple cellular alterations that impinge upon transport efficiency. Under normal conditions, we find that the mRNA export receptor Mex67 and Nab2 directly interact. However, upon heat shock stress, Mex67 does not localize to the Mlp1 nuclear foci, and its association with Nab2 complexes is reduced. These results reveal a novel mechanism by which the MAP kinase Slt2 and Mlp1 control mRNA export factors during heat shock stress.
机译：细胞对环境压力条件的适应性要求基因表达快速而具体地变化。在热激过程中，大多数聚腺苷酸化的mRNA被保留在细胞核中，而热激诱导的mRNA则被允许输出。尽管已知必需的mRNA输出因子，但尚未完全了解调节转运的确切机制。在这里，我们发现在酿酒酵母（Saccharomyces cerevisiae）热休克期间，mRNA结合蛋白Nab2在丝氨酸178和丝氨酸180上被丝裂原激活蛋白（MAP）激酶Slt2 / Mpk1磷酸化。 Slt2是热休克后核聚（A + ）mRNA积累所必需的，而 nup42 nab2-T178A / S180A 突变体的耐热性降低。与磷酸化巧合的是，Nab2和Yra1与Mlp1（一种参与mRNA保留的蛋白质）在核灶中共定位。 Nab2核焦点形成和Nab2磷酸化是独立的，表明热激诱导多种细胞改变，这些改变影响运输效率。在正常条件下，我们发现mRNA出口受体Mex67和Nab2直接相互作用。但是，在热激胁迫下，Mex67不会定位于Mlp1核病灶，并且其与Nab2配合物的缔合也降低了。这些结果揭示了一种新的机制，通过该机制，MAP激酶Slt2和Mlp1在热激应激过程中控制mRNA输出因子。

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