首页> 外文OA文献 >Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
【2h】

Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport

机译:肌球蛋白运动而不是肌动蛋白彗星是基于肌动蛋白的高尔基体向内质网蛋白运输的介质

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。

摘要

We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibitors such as 2,3-butanedione monoxime (BDM) and 1-[5-isoquinoline sulfonyl]-2-methyl piperazine (ML7), which inhibit myosin and the phosphorylation of myosin II by the myosin light chain kinase, respectively; and a mutant of the nonmuscle myosin II regulatory light chain, which cannot be phosphorylated (MRLC2AA). On the other hand, actin comet tails were induced by the overexpression of phosphatidylinositol phosphate 5-kinase. Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the brefeldin A (BFA)-induced fusion of Golgi enzymes with the endoplasmic reticulum (ER). This delay was not caused by an alteration in the formation of the BFA-induced tubules from the Golgi complex. In addition, the Shiga toxin fragment B transport from the Golgi complex to the ER was also altered. This impairment in the retrograde protein transport was not due to depletion of intracellular calcium stores or to the activation of Rho kinase. Neither the reassembly of the Golgi complex after BFA removal nor VSV-G transport from ER to the Golgi was altered in cells treated with BDM/ML7 or expressing MRLC2AA. Finally, transport carriers containing Shiga toxin did not move into the cytosol at the tips of comet tails of polymerizing actin. Collectively, the results indicate that 1) myosin motors move to transport carriers from the Golgi complex to the ER along actin filaments; 2) nonmuscle myosin II mediates in this process; and 3) actin comets are not involved in retrograde transport.
机译:先前我们曾报道肌动蛋白丝参与蛋白质从高尔基体到内质网的运输。在这里,我们检查了肌球蛋白电机或肌动蛋白彗星是否介导这种运输。为了解决这个问题,我们一方面使用了特定抑制剂的组合,例如2,3-丁二酮单肟(BDM)和1- [5-异喹啉磺酰基] -2-甲基哌嗪(ML7),它们抑制肌球蛋白和肌球蛋白轻链激酶分别使肌球蛋白II磷酸化;非肌球蛋白II调节轻链的突变体,该突变体不能被磷酸化(MRLC2AA)。另一方面,肌动蛋白彗星尾巴是由磷脂酰肌醇磷酸5-激酶的过表达诱导的。用BDM / ML7处理的细胞或表达MRLC2AA突变的细胞显示,布雷菲德菌素A(BFA)诱导的高尔基酶与内质网(ER)融合显着减少。这种延迟不是由高尔基复合体中BFA诱导的小管形成的改变引起的。另外,志贺毒素片段B从高尔基体向ER的转运也被改变。逆行蛋白质运输中的这种损害不是由于细胞内钙存储的耗尽或Rho激酶的激活引起的。在用BDM / ML7处理或表达MRLC2AA的细胞中,去除BFA后高尔基复合体的重组和从ER到高尔基的VSV-G转运都没有改变。最后,含有志贺毒素的转运载体没有在聚合肌动蛋白彗尾的尖端移入胞质溶胶。总体而言,结果表明:1)肌球蛋白电机移动,将肌动蛋白丝将载体从高尔基复合体转运至内质网; 2)非肌肉肌球蛋白II在此过程中介导; 3)肌动蛋白彗星不参与逆行运输。

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