Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Golgi Matrix Proteins01:12

Golgi 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...
2.1K
Transport Across the Golgi01:26

Transport 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
Golgi Apparatus01:49

Golgi 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
ER Retrieval Pathway01:45

ER 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...
3.9K
Export of Misfolded Proteins out of the ER01:32

Export 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
Vesicular Tubular Clusters01:45

Vesicular 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...
2.6K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Multi-center validation of a machine learning model for early detection of monoclonal immunoglobulin-related disorders using routine laboratory data.

Frontiers in immunology·2026
Same author

Targeting androgen receptor transcriptionally represses VCP and enhances the efficacy of oncolytic-immunotherapy in hepatocellular carcinoma.

Pharmacological research·2026
Same author

Mitotic Cdc42 waves encode PI(3,4)P<sub>2</sub> signaling and Golgi morphological state to control spindle scaling.

Science advances·2026
Same author

Characterizing selection signatures in coding and noncoding regions of 14,886 cancer genomes.

Journal of genetics and genomics = Yi chuan xue bao·2026
Same author

Coordinated changes in microbiota features, short-chain fatty acids, and peripheral clocks accompany fructo-oligosaccharide-associated metabolic improvement.

Food & function·2026
Same author

[Impact of effective health information acquisition on hemophilia-related health literacy among caregivers of underage hemophilia patients].

Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences·2026
Same journal

A tri-axis optomechanical accelerometer with plasmonic MIM waveguide and structural direction-dependent optical signatures.

Scientific reports·2026
Same journal

Holographic leaky-wave antennas with independently controlled multiple counter-rotating vortex beams.

Scientific reports·2026
Same journal

Differential associations of longitudinal hearing and vision trajectories with dementia and mild cognitive impairment in older adults.

Scientific reports·2026
Same journal

Abdominal obesity and leisure-time sedentary behavior in relation to gastroesophageal reflux disease risk: a prospective cohort study from the UK Biobank.

Scientific reports·2026
Same journal

Effect of nitrogen-rich COF incorporation on the structure and separation performance of polyamide nanofiltration membranes.

Scientific reports·2026
Same journal

Withanolide A inhibits hIAPP aggregation: An In silico, biophysical, and drosophila-based In vivo validation.

Scientific reports·2026
See all related articles

Related Experiment Video

Updated: Aug 30, 2025

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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
PubMed
Summary
This summary is machine-generated.

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.

More Related Videos

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

10.9K
4D Microscopy of Yeast
12:00

4D Microscopy of Yeast

Published on: April 28, 2019

8.7K

Related Experiment Videos

Last Updated: Aug 30, 2025

Analysis of Endocytic Uptake and Retrograde Transport to the Trans-Golgi Network Using Functionalized Nanobodies in Cultured Cells
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
Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
13:08

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass

Published on: August 10, 2017

10.9K
4D Microscopy of Yeast
12:00

4D Microscopy of Yeast

Published on: April 28, 2019

8.7K

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.