• 主题
高级搜索  >
历史搜索 清空历史
首页> 美国卫生研究院文献>Cell Regulation >Multiple Sequence Elements Facilitate Chp Rho GTPase Subcellular Location Membrane Association and Transforming Activity
【2h】

Multiple Sequence Elements Facilitate Chp Rho GTPase Subcellular Location Membrane Association and Transforming Activity

机译：多个序列元件可促进Chp Rho GTPase亚细胞定位膜结合和转化活性

代理获取
本网站仅为用户提供外文OA文献查询和代理获取服务，本网站没有原文。下单后我们将采用程序或人工为您竭诚获取高质量的原文，但由于OA文献来源多样且变更频繁，仍可能出现获取不到、文献不完整或与标题不符等情况，如果获取不到我们将提供退款服务。请知悉。
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Cdc42 homologous protein (Chp) is a member of the Rho family of small GTPases and shares significant sequence and functional similarity with Cdc42. However, unlike classical Rho GTPases, we recently found that Chp depends on palmitoylation, rather than prenylation, for association with cellular membranes. Because palmitoylation alone is typically not sufficient to promote membrane association, we evaluated the possibility that other carboxy-terminal residues facilitate Chp subcellular association with membranes. We found that Chp membrane association and transforming activity was dependent on the integrity of a stretch of basic amino acids in the carboxy terminus of Chp and that the basic amino acids were not simply part of a palmitoyl acyltransferase recognition motif. We also determined that the 11 carboxy-terminal residues alone were sufficient to promote Chp plasma and endomembrane association. Interestingly, stimulation with tumor necrosis factor-α activated only endomembrane-associated Chp. Finally, we found that Chp membrane association was not disrupted by Rho guanine nucleotide dissociation inhibitory proteins, which are negative regulators of Cdc42 membrane association and biological activity. In summary, the unique carboxy-terminal sequence elements that promote Chp subcellular location and function expand the complexity of mechanisms by which the cellular functions of Rho GTPases are regulated.
机译：Cdc42同源蛋白（Chp）是小型GTPases的Rho家族的成员，与Cdc42具有重要的序列和功能相似性。但是，与经典的Rho GTPases不同，我们最近发现Chp与细胞膜的结合依赖于棕榈酰化而不是异戊二烯化。因为单独的棕榈酰化通常不足以促进膜缔合，所以我们评估了其他羧基末端残基促进Chp与膜亚细胞缔合的可能性。我们发现Chp膜的缔合和转化活性取决于在Chp羧基末端的一连串碱性氨基酸的完整性，并且碱性氨基酸不只是棕榈酰酰基转移酶识别基序的一部分。我们还确定单独的11个羧基末端残基足以促进Chp血浆和内膜结合。有趣的是，用肿瘤坏死因子-α刺激仅激活了与膜相关的Chp。最后，我们发现Chp膜结合并未被Rho鸟嘌呤核苷酸解离抑制蛋白破坏，Rho鸟嘌呤核苷酸解离抑制蛋白是Cdc42膜结合和生物活性的负调节剂。总之，促进Chp亚细胞定位和功能的独特的羧基末端序列元件扩展了调节Rho GTPases细胞功能的机制的复杂性。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
代理获取

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