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Protein Glycosylation

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...

Oligosaccharide Assembly

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...

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Related Experiment Video

Updated: Sep 20, 2025

Glycan Profiling of Plant Cell Wall Polymers using Microarrays

Glycan Profiling of Plant Cell Wall Polymers using Microarrays

Published on: December 17, 2012

Applying transcriptomics to studyglycosylation at the cell type level.

Leo Alexander Dworkin¹, Henrik Clausen¹, Hiren Jitendra Joshi¹

¹Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, 2200 Copenhagen N, Denmark.

|June 6, 2022

Summary

This summary is machine-generated.

This study uses single-cell RNA sequencing to analyze the cellular glycosylation machinery. Glycopacity software identifies key enzymes as regulatory hotspots in the glycome, advancing single-cell glycosylation analysis.

Keywords:

Molecular biology Omics Transcriptomics

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Area of Science:

Biochemistry
Systems Biology
Genomics

Background:

Glycosylation is a crucial cellular process, but its single-cell output (glycome) is difficult to measure.
Existing analytical methods struggle to capture the complexity of glycosylation at the single-cell level.

Purpose of the Study:

To investigate the use of single-cell RNA sequencing (scRNA-seq) data for characterizing the glycosylation machinery and metabolic network within individual cells.
To identify transcriptionally regulated enzymes as potential control points (hotspots) in cellular glycosylation.

Main Methods:

Analysis of differential mRNA regulation for 214 glycosylation and modification enzymes using scRNA-seq data.
Development and application of the Glycopacity software to interpret transcriptome data for glycosylation insights.

Main Results:

Most enzymes involved in producing general oligosaccharide scaffolds show limited transcriptional regulation across cells.
Key enzymes within specific glycosylation pathways were identified as highly transcriptionally regulated hotspots.
Glycopacity software successfully extracts and interprets glycosylation information from transcriptome data.

Conclusions:

scRNA-seq data can effectively characterize the single-cell glycosylation machinery and metabolic network.
Identifying transcriptionally regulated enzymes provides insights into controlling the cellular glycome.
The Glycopacity software is a valuable tool for analyzing glycosylation from transcriptomic data.