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相关概念视频

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

12.1K
The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

4.5K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
4.5K
ER Retrieval Pathway01:45

ER Retrieval Pathway

3.8K
In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.8K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.5K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.5K

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相关实验视频

Updated: Jun 7, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells

Published on: February 18, 2014

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在体内可视化ER-phagy和ER架构.

Yongjuan Sang1,2, Boran Li1, Tinglin Su1

  • 1International Institutes of Medicine, The Fourth Affiliated Hospital of Zhejiang University School of Medicine , Yiwu, China.

The Journal of cell biology
|November 18, 2024
PubMed
概括

研究人员开发了新的小鼠模型来研究ER-phagy (内质网膜自). 这些模型揭示了ER-phagy在体内如何变化以及在压力期间的变化,为细胞健康提供了洞察力.

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科学领域:

  • 细胞生物学 细胞生物学
  • 分子生物学分子生物学
  • 自学研究 自学研究

背景情况:

  • ER-phagy对于细胞平衡至关重要,但其变异和疾病相关性尚不清楚.
  • 需要可量化的体内方法来研究ER结构和ER-phagy动态.
  • 现有的知识差距阻碍了对ER-phagy在不同细胞类型和病理中的作用的理解.

研究的目的:

  • 开发新的记者小鼠模型,以在体内可视化和量化ER-phagy和ER架构.
  • 研究不同器官和组织的ER-phagy的时空变异.
  • 在各种压力条件下探索ER-phagy和ER网络的改造.

主要方法:

  • 产生两个转基因小鼠系表达ER光定位并列RFP-GFP (ER-TRG) 标签.
  • 为精确的时间控制,ER-TRG标签的组成和条件表达式.
  • 在不同器官,组织和初级培养中体内和体外对ER-phagy和ER结构的系统分析.

主要成果:

  • 在不同器官和组织中观察到基底ER-phagy水平的显著变化.
  • 在饥饿和受伤等压力条件下,ER-phagy和ER网络架构经历了实质性的改造.
  • 该ER-TRG报告员系统允许在体内测量ER-phagy的单细胞分辨率.

结论:

  • 开发的ER-TRG记者小鼠模型是研究ER-phagy的宝贵工具.
  • 这些模型促进了对细胞平衡和ER动态的基础研究.
  • 这些发现在各种疾病的翻译研究中具有广泛的应用.