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Related Concept Videos

Golgi Apparatus01:49

Golgi Apparatus

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.
Golgi Apparatus01:09

Golgi Apparatus

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...
Golgi Apparatus01:09

Golgi Apparatus

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...
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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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

Re'COG'nition at the Golgi.

Victoria J Miller1, Daniel Ungar

  • 1Department of Biology, University of York, York, UK.

Traffic (Copenhagen, Denmark)
|February 4, 2012
PubMed
Summary
This summary is machine-generated.

The conserved oligomeric Golgi (COG) complex is crucial for retrograde vesicle transport, maintaining Golgi glycosylation homeostasis. Advances in understanding COG structure and function illuminate its role in tethering complexes and human glycosylation disorders.

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Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The conserved oligomeric Golgi (COG) complex regulates retrograde vesicle transport within the Golgi apparatus.
  • COG is essential for maintaining glycosylation homeostasis by controlling the distribution of glycosylation enzymes.
  • Recent structural and functional studies have significantly advanced our understanding of the COG complex.

Purpose of the Study:

  • To review the current knowledge of the COG complex's involvement in Golgi vesicle tethering.
  • To explore how COG complex structure and function impact molecular understanding of vesicle tethering.
  • To discuss the implications of COG complex research for Golgi function and human glycosylation disorders.

Main Methods:

  • Literature review of recent studies on COG complex composition, interactions, function, and structure.
  • Analysis of structural data placing COG within the family of multi-subunit tethering complexes.
  • Integration of findings related to COG-dependent human glycosylation disorders.

Main Results:

  • The COG complex plays a vital role in coordinating retrograde vesicle transport at the Golgi.
  • Structural data confirm COG as a member of the multi-subunit tethering complex family, alongside exocyst, Dsl1, and GARP.
  • COG's function is directly linked to the precise distribution of glycosylation enzymes, impacting cellular glycosylation.

Conclusions:

  • Understanding COG's role in vesicle tethering provides molecular insights into Golgi dynamics.
  • The COG complex is critical for fine-tuning Golgi function, particularly glycosylation processes.
  • Research on the COG complex has significant implications for understanding and potentially treating human glycosylation disorders.