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

2.5K
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
Golgi Apparatus01:49

Golgi Apparatus

105.3K
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.
105.3K
Golgi Apparatus01:09

Golgi Apparatus

22.4K
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...
22.4K
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

4.5K
Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
4.5K
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

5.6K
GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
5.6K
Transport Across the Golgi01:26

Transport Across the Golgi

6.3K
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...
6.3K

You might also read

Related Articles

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

Sort by
Same author

COG Complex in Golgi Trafficking and Glycosylation.

Sub-cellular biochemistry·2026
Same author

Deep proteomic profiling of the intra-Golgi trafficking intermediates.

Molecular biology of the cell·2025
Same author

Acute GARP Depletion Disrupts Vesicle Transport, Leading to Severe Defects in Sorting, Secretion and O-Glycosylation.

Traffic (Copenhagen, Denmark)·2025
Same author

Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates.

bioRxiv : the preprint server for biology·2024
Same author

Acute GARP depletion disrupts vesicle transport, leading to severe defects in sorting, secretion, and O-glycosylation.

bioRxiv : the preprint server for biology·2024
Same author

Essential role of the conserved oligomeric Golgi complex in <i>Toxoplasma gondii</i>.

mBio·2023
Same journal

Future Directions in Biotechnological and Pharmacological Applications of CAIs.

Sub-cellular biochemistry·2026
Same journal

Industrial and Environmental Applications of Carbonic Anhydrases.

Sub-cellular biochemistry·2026
Same journal

Applications of Carbonic Anhydrase Inhibitors in Arthritis, Neuropathic Pain, Acute Mountain Sickness, and Cerebral Ischemia.

Sub-cellular biochemistry·2026
Same journal

Applications of Carbonic Anhydrase Inhibitors in Neurological Disorders, Mechanisms and Therapeutic Potential.

Sub-cellular biochemistry·2026
Same journal

Carbonic Anhydrase Inhibitors in Oncology.

Sub-cellular biochemistry·2026
Same journal

Therapeutic Applications of Carbonic Anhydrase Inhibitors in Ophthalmology.

Sub-cellular biochemistry·2026
See all related articles

Related Experiment Video

Updated: Feb 22, 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

GARP Complex in Golgi Physiology.

Amrita Khakurel1, Walter S Aragon-Ramirez1, Vladimir V Lupashin2

  • 1Department of Physiology and Cell Biology, University of Arkansas for Medical Sciences, Little Rock, AR, USA.

Sub-Cellular Biochemistry
|February 20, 2026
PubMed
Summary
This summary is machine-generated.

The Golgi Associated Retrograde Protein (GARP) complex is crucial for vesicle transport from endosomes to the Golgi. Understanding GARP

Keywords:
Endosome-TGN retrograde traffickingGARPGlycosylationTrafficking machineryVesicle tethering

More Related Videos

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

9.7K
Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

18.8K

Related Experiment Videos

Last Updated: Feb 22, 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
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

9.7K
Visualization of G3BP Stress Granules Dynamics in Live Primary Cells
10:12

Visualization of G3BP Stress Granules Dynamics in Live Primary Cells

Published on: May 21, 2014

18.8K

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • The Golgi Associated Retrograde Protein (GARP) complex, part of the CATCHR family, mediates vesicle tethering from endosomes to the trans-Golgi network (TGN).
  • GARP is vital for sorting hydrolases and recycling membrane proteins but its precise mechanisms, partners, and trafficking intermediates are understudied.
  • GARP-dependent pathways are used by recycling proteins, hydrolase receptors, and pathogens, with mutations linked to neurological disorders.

Purpose of the Study:

  • To review the current knowledge on the structure, function, and interactions of the GARP complex.
  • To summarize the impact of GARP mutations and their association with human pathologies.
  • To highlight the understudied aspects of GARP-dependent trafficking.

Main Methods:

  • Literature review of existing studies on the GARP complex.
  • Analysis of research on GARP's role in protein sorting and membrane recycling.
  • Compilation of data on GARP mutations and associated neurological disorders in humans and model organisms.

Main Results:

  • GARP complex functions in endosome-to-TGN retrograde trafficking.
  • GARP-dependent transport is essential for various cellular processes and exploited by pathogens.
  • Mutations in GARP subunits are implicated in neurological diseases, though mechanisms are unclear.

Conclusions:

  • The GARP complex plays a critical role in cellular trafficking pathways.
  • Further research is needed to elucidate GARP's exact molecular mechanisms and disease associations.
  • Understanding GARP is vital for insights into both normal cell function and neurological disorder pathogenesis.