Related Experiment Video
Updated: Aug 30, 2025
11:05
Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
Published on: February 21, 2019
9.2K
Retro-2 alters Golgi structure
Xihua Yue1, Bopil Gim2, Lianhui Zhu1
1School of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Scientific Reports
|September 2, 2022
Summary
Retro-2 disrupts the Golgi apparatus by causing vesicular accumulation and disassembly. This occurs rapidly, even in cells lacking key Golgi structural proteins, revealing a profound impact on cellular organization.
Area of Science:
- Cell Biology
- Molecular Biology
- Structural Biology
Background:
- The Golgi apparatus is crucial for protein modification and transport.
- SARS-CoV-2 infection disrupts the Golgi, but the mechanism is unclear.
- Retro-2 inhibits SARS-CoV-2 replication by affecting ER exit site protein Sec16A and Golgi tSNARE Syntaxin5.
Purpose of the Study:
- To investigate the ultrastructural effects of Retro-2 on the Golgi apparatus.
- To understand how Retro-2 influences Golgi organization and protein transport.
Main Methods:
- Electron microscopy (EM) and EM tomography were used to analyze Golgi ultrastructure.
- Protein secretion assays were performed to assess cargo transport.
- Experiments involved Retro-2 treatment in cells with and without GRASP65/55 proteins.
Main Results:
- Retro-2 treatment did not significantly affect secretion of small or large cargos.
- Ultrastructural analysis revealed rapid accumulation of COPI-like vesicles and partial Golgi stack disassembly within 3-5 hours.
- In GRASP65/55-depleted cells, Retro-2 induced complete and rapid Golgi disassembly into individual cisternae.
Conclusions:
- Retro-2 profoundly alters Golgi structure, leading to rapid disorganization.
- The drug's effect on Golgi ultrastructure is more significant than previously understood.
- These findings provide insights into Golgi dynamics and potential therapeutic targets.
Related Concept Videos
01:12Golgi Matrix Proteins
2.1K
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.1K
01:26Transport Across the Golgi
4.4K
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
4.4K
01:49Golgi Apparatus
91.6K
As they leave the Endoplasmic Reticulum (ER), properly folded and assembled proteins are selectively packaged into vesicles. These vesicles are transported by microtubule-based motor proteins and fuse together to form vesicular tubular clusters, subsequently arriving at the Golgi apparatus, a eukaryotic endomembrane organelle that often has a distinctive ribbon-like appearance.
91.6K
01:45ER Retrieval Pathway
3.9K
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...
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
3.9K
01:32Export of Misfolded Proteins out of the ER
3.8K
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...
3.8K
01:45Vesicular Tubular Clusters
2.6K
After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
With the help of motor proteins such...
2.6K