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 Apparatus01:49

Golgi Apparatus

104.9K
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.
104.9K
Golgi Apparatus01:09

Golgi Apparatus

22.3K
Properly folded and assembled proteins are selectively packaged into vesicles that exit the ER. Motor proteins transport these vesicles to the Golgi apparatus for adding modifications that make these proteins functional at their destination.
The Golgi apparatus is a eukaryotic organelle that has a distinctive ribbon-like appearance. It is a primary sorting and dispatch station for cargo arriving from the ER. Newly arriving vesicles enter the cis face of the Golgi, closest to the ER, and are...
22.3K
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

2.5K
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...
2.5K
Transport Across the Golgi01:26

Transport Across the Golgi

6.2K
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...
6.2K
Protein Glycosylation01:25

Protein Glycosylation

9.8K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
9.8K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.7K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.7K

You might also read

Related Articles

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

Sort by
Same author

The hypoxic response extends lifespan through a bioaminergic and peptidergic neural circuit.

bioRxiv : the preprint server for biology·2025
Same author

SARS-CoV-2 remodels the Golgi apparatus to facilitate viral assembly and secretion.

PLoS pathogens·2025
Same author

Deguelin promotes longevity and healthspan through <i>C. elegans fmo-4</i>.

microPublication biology·2025
Same author

GRASP55 regulates sorting and maturation of the lysosomal enzyme β-hexosaminidase A.

Molecular biology of the cell·2025
Same author

The Fourth Annual Symposium of the Midwest Aging Consortium.

The journals of gerontology. Series A, Biological sciences and medical sciences·2024
Same author

GRASP55 Regulates Sorting and Maturation of the Lysosomal Enzyme β-Hexosaminidase A.

bioRxiv : the preprint server for biology·2024

Related Experiment Video

Updated: Feb 17, 2026

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

11.4K

Golgi structure formation, function, and post-translational modifications in mammalian cells.

Shijiao Huang1, Yanzhuang Wang1

  • 1Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.

F1000Research
|December 12, 2017
PubMed
Summary

The Golgi apparatus, crucial for protein modification and transport, dynamically alters its structure. Post-translational modifications like phosphorylation and ubiquitination significantly impact Golgi architecture and function.

Keywords:
Golgi apparatusGolgi membrane dynamicscell cycleformationstructure

More Related Videos

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.1K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.2K

Related Experiment Videos

Last Updated: Feb 17, 2026

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

11.4K
Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
11:25

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

Published on: October 4, 2017

7.1K
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
08:58

Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

13.2K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The Golgi apparatus is a vital organelle for protein and lipid trafficking and post-translational modifications.
  • In mammalian cells, it forms ribbon-like structures from stacked cisternae in the perinuclear region.
  • Golgi structure is dynamic, changing with the cell cycle and disease states.

Purpose of the Study:

  • To review the relationship between Golgi structure, function, and regulation.
  • To focus on how post-translational modifications influence Golgi architecture.
  • To examine the effects of Golgi unstacking on cellular functions.

Main Methods:

  • Literature review and synthesis of current research.
  • Analysis of studies on protein phosphorylation and ubiquitination.
  • Examination of data on Golgi unstacking and its functional consequences.

Main Results:

  • Post-translational modifications, specifically phosphorylation and ubiquitination, are key regulators of Golgi structure.
  • Golgi unstacking disrupts essential functions including protein trafficking, glycosylation, and sorting.
  • Maintaining Golgi integrity is critical for cellular processes.

Conclusions:

  • Understanding Golgi structure-function dynamics is essential for cell biology.
  • Dysregulation of Golgi structure by post-translational modifications has significant functional implications.
  • Further research into Golgi regulation can inform disease mechanisms and therapeutic strategies.