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Updated: Jun 7, 2025

Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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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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相关概念视频

The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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 Membrane

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Sec61 protein conducting channel
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ER Retrieval Pathway

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.
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Export of Misfolded Proteins out of the ER01:32

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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...
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