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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...

Notch Signaling Pathway

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Notch Signaling Pathway

Notch Signaling Pathway

The Notch signaling pathway is a major intracellular signaling pathway that is highly conserved over a broad spectrum of metazoan species. It stands unique from other intracellular signaling mechanisms in animals because notch protein itself acts as the receptor as well as the primary signaling molecule.
The Notch gene came into the limelight in 1914 after the discovery that its mutation in Drosophila melanogaster leads to a serrated (or "notched") wing margin phenotype. It was not until 1985...

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
Direct cell-to-cell contact is needed for the activation of Notch signaling. The signal is initiated when a notch ligand binds to a receptor on an adjacent cell, also...

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Related Experiment Video

Updated: Jun 17, 2026

Stimulation of Notch Signaling in Mouse Osteoclast Precursors

Stimulation of Notch Signaling in Mouse Osteoclast Precursors

Published on: February 28, 2017

Glycosylation regulates Notch signalling.

Nicola Haines¹, Kenneth D Irvine

¹Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers: The State University of New Jersey, Piscataway, New Jersey 08854, USA.

Nature Reviews. Molecular Cell Biology

|October 23, 2003

Summary

Glycosylation, an extracellular modification, is crucial for intercellular signaling. Differences in glycosylation levels significantly regulate the Notch signaling pathway, a key area of ongoing research.

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Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Intracellular post-translational modifications like phosphorylation and ubiquitylation are well-understood regulators of cell signaling.
The role of extracellular modifications, particularly glycosylation, in intercellular signaling is an emerging field of study.

Purpose of the Study:

To elucidate the regulatory role of differential glycosylation in intercellular signaling.
To highlight the importance of glycosylation in the context of the Notch signaling pathway.

Main Methods:

Review of recent studies on post-translational modifications.
Analysis of glycosylation patterns in intercellular communication.

Main Results:

Extracellular glycosylation is essential for the proper functioning of the Notch signaling pathway.
Variations in the extent of glycosylation represent a key regulatory mechanism for Notch signaling.

Conclusions:

Glycosylation is a critical extracellular post-translational modification that significantly impacts intercellular signaling.
Understanding differential glycosylation is key to comprehending the regulation of pathways like Notch signaling.