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Related Concept Videos

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 Glycosylation01:25

Protein Glycosylation

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...
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...
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.The Golgi apparatus is a major sorting and dispatch station for the products of the ER. Newly arriving vesicles enter...
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...

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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

Golgi glycosylation.

Pamela Stanley1

  • 1Department of Cell Biology, Albert Einstein College of Medicine, New York, New York 10461, USA. pamela.stanley@einstein.yu.edu

Cold Spring Harbor Perspectives in Biology
|March 29, 2011
PubMed
Summary
This summary is machine-generated.

Glycosylation, a key protein and lipid modification, primarily occurs in the Golgi apparatus. This process involves ordered enzymes and is influenced by cellular conditions, impacting glycan diversity.

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Last Updated: Jun 3, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
10:17

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

Published on: April 27, 2010

Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Glycosylation is a crucial post-translational modification for proteins and lipids.
  • Initial glycosylation occurs in the ER, but mature glycan synthesis is completed in the Golgi apparatus.
  • Golgi membranes contain an ordered array of enzymes and transporters essential for sequential glycan processing.

Purpose of the Study:

  • To elucidate the mechanisms and regulation of glycosylation within the Golgi apparatus.
  • To understand how cellular factors influence the diversity of glycan structures.
  • To highlight the applications of Golgi glycosylation knowledge in biological research.

Main Methods:

  • Analysis of Golgi-resident enzymes (glycosyltransferases, glycosidases) and nucleotide sugar transporters.
  • Investigation of factors affecting glycosylation, including Golgi pH, protein integrity, signaling, and stress.
  • Utilizing knowledge of Golgi glycosylation for developing research assays and engineering glycoproteins.

Main Results:

  • Most glycosylation reactions, particularly the addition of diverse sugars to form mature glycans, occur in the Golgi.
  • The specific set of glycosylation enzymes varies by cell type, leading to diverse glycan structures on glycoconjugates.
  • Glycan synthesis is modulated by Golgi pH, protein interactions, signaling pathways, membrane dynamics, and cellular stress.

Conclusions:

  • The Golgi apparatus is the central site for complex glycan synthesis and maturation.
  • Cellular context and environmental factors significantly influence the outcome of glycosylation.
  • Understanding Golgi glycosylation aids in studying intracellular trafficking and engineering glycoproteins.