首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >The Gp78 ubiquitin ligase: Probing endoplasmic reticulum complexity
【24h】

The Gp78 ubiquitin ligase: Probing endoplasmic reticulum complexity

机译:Gp78泛素连接酶:探索内质网的复杂性

获取原文
获取原文并翻译 | 示例
           

摘要

The endoplasmic reticulum (ER) has been classically divided, based on electron microscopy analysis, into parallel ribosome-studded rough ER sheets and a tubular smooth ER network. Recent studies have identified molecular constituents of the ER, the reticulons and DP1, that drive ER tubule formation and whose expression determines expression of ER sheets and tubules and thereby rough and smooth ER. However, segregation of the ER into only two domains remains simplistic and multiple functionally distinct ER domains necessarily exist. In this review, we will discuss the sub-organization of the ER in different domains focusing on the localization and role of the gp78 ubiquitin ligase in the mitochondria-associated smooth ER and on the evidence for a quality control ERAD domain.
机译:基于电子显微镜分析,内质网(ER)已经典地分为散布有平行核糖体的粗糙ER薄片和管状光滑ER网络。最近的研究已经确定了内质网,网状结构和DP1的分子成分,这些分子驱动内质网的形成,其表达决定了内质网片和小管的表达,从而决定了内质网的粗糙和光滑。然而,将ER仅分成两个结构域仍然是简单的,并且必然存在多个功能不同的ER结构域。在这篇综述中,我们将讨论ER在不同域中的亚组织,重点是gp78泛素连接酶在线粒体相关平滑ER中的定位和作用,以及对质量控制ERAD域的证据。

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