• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>American Journal of Physiology >Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70.
【24h】

Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70.

机译：压力抑制热休克蛋白hsc70的核质穿梭。

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

Heat shock proteins of the hsp/hsc70 family are essential chaperones, implicated in the stress response, aging, and a growing number of human diseases. At the molecular level, hsc70s are required for the proper folding and intracellular targeting of polypeptides as well as the regulation of apoptosis. Cytoplasmic members of the hsp/hsc70 family are believed to shuttle between nuclei and cytoplasm; they are found in both compartments of unstressed cells. Our experiments demonstrate that actin filament-destabilizing drugs trigger the nuclear accumulation of hsc70s in unstressed and heat-shocked cells recovering from stress. Using human-mouse heterokaryons, we show that stress inhibits shuttling and sequesters the chaperone in nuclei. The inhibition of hsc70 shuttling upon heat shock is only transient, and transport is reestablished when cells recover from stress. Hsc70 shuttling is controlled by hsc70 retention in the nucleus, a process that is mediated by two distinct mechanisms, ATP-sensitive binding of hsc70s to chaperone substrates and, furthermore, the association with nucleoli. The nucleolar protein fibrillarin and ribosomal protein rpS6 were identified as components that show an increased association with hsc70s in the nucleus upon stress exposure. Together, our data suggest that stress abolishes the exit of hsc70s from the nucleus to the cytoplasm, thereby limiting their function to the nuclear compartment. We propose that during recovery from stress hsc70s are released from nuclear and nucleolar anchors, which is a prerequisite to restore shuttling.
机译：hsp / hsc70家族的热激蛋白是必不可少的伴侣，与应激反应，衰老和越来越多的人类疾病有关。在分子水平上，hsc70s是多肽正确折叠和细胞内靶向以及调节细胞凋亡所必需的。 hsp / hsc70家族的细胞质成员被认为在细胞核和细胞质之间穿梭。它们都在未受压细胞的两个隔室中发现。我们的实验表明，肌动蛋白丝破坏性药物触发了从应激中恢复的无应力和热休克细胞中hsc70s的核积累。我们使用人类小鼠异核体，表明压力抑制穿梭和隔离分子中的伴侣分子。热休克对hsc70穿梭的抑制作用只是暂时的，当细胞从压力中恢复时，转运重新建立。 Hsc70穿梭受hsc70保留在细胞核中的控制，该过程由两种不同的机制介导，即hsc70s与伴侣底物的ATP敏感结合以及与核仁的缔合。核仁蛋白原纤维蛋白和核糖体蛋白rpS6被鉴定为在压力暴露下与核中hsc70s关联增加的组分。在一起，我们的数据表明，压力消除了hsc70s从细胞核到细胞质的出口，从而限制了它们在核区室的功能。我们建议从应力恢复过程中，hsc70s从核锚和核仁锚中释放，这是恢复穿梭的先决条件。

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