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Transport Across the Golgi

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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...

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Related Experiment Video

Updated: Jun 8, 2025

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

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

Published on: August 10, 2017

Comprehensive Proteomic Characterization of the Intra-Golgi Trafficking Intermediates.

Farhana Taher Sumya¹, Walter S Aragon-Ramirez¹, Vladimir V Lupashin¹

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

Biorxiv : the Preprint Server for Biology

|November 1, 2024

Summary

The Conserved Oligomeric Golgi (COG) complex is crucial for recycling glycosylation machinery within Golgi vesicles. COG dysfunction disrupts intra-Golgi sorting by impairing vesicle tethering and uncoating.

Keywords:

COG complex Golgi SNARE degron glycosylation mass-spectrometry vesicle tethering vesicular coat vesicular trafficking

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Published on: August 16, 2021

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Intracellular trafficking utilizes vesicular intermediates, but their precise function in the Golgi apparatus remains unclear.
The Conserved Oligomeric Golgi (COG) complex plays a role in Golgi function, yet its specific mechanisms are debated.

Purpose of the Study:

To investigate the role of the COG complex in Golgi vesicle trafficking and intra-Golgi sorting.
To elucidate the molecular composition and dynamics of Golgi-derived vesicles under conditions of COG dysfunction.

Main Methods:

Induction of acute COG complex dysfunction in cells.
Proteomic analysis of vesicles isolated from cis, medial, and trans-Golgi compartments.
Comparative analysis of vesicle molecular profiles in wild-type versus COG-depleted cells.

Main Results:

Wild-type Golgi vesicles exhibit distinct molecular profiles, indicative of efficient Golgi protein recycling.
COG depletion leads to accelerated vesicle uncoating and increased overlap in vesicle molecular profiles.
The entire Golgi glycosylation machinery is shown to recycle via vesicles in a COG-dependent manner.

Conclusions:

The COG complex is essential for orchestrating the multi-step recycling of Golgi glycosylation machinery.
Defects in vesicle tethering, caused by COG dysfunction, disrupt intra-Golgi sorting.
Specific Golgi coats, tethers, Rabs, and SNAREs coordinate COG-dependent glycosylation machinery recycling.