protein O-linked glycosylation via threonine

Definition

Target type: biologicalprocess

The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine. [RESID:AA0155]

Protein O-linked glycosylation via threonine is a post-translational modification where a sugar molecule is attached to the hydroxyl group of a threonine residue in a protein. This process is distinct from N-linked glycosylation, which occurs on asparagine residues.

The process typically begins with the activation of a sugar molecule, often N-acetylglucosamine (GlcNAc), by a specific enzyme called a glycosyltransferase. The activated sugar molecule is then transferred to the hydroxyl group of threonine by another glycosyltransferase, forming an O-linked glycosidic bond. The specific glycosyltransferase involved in this process determines the type of sugar added.

After the initial glycosylation event, the O-linked glycan can be further modified by the addition of other sugars, resulting in complex oligosaccharide structures. These modifications are carried out by a variety of glycosyltransferases and glycosidases.

O-linked glycosylation via threonine plays a critical role in various cellular processes, including:

* **Protein folding and stability:** O-linked glycosylation can influence the conformation and stability of proteins, contributing to their proper function.
* **Cellular signaling:** O-linked glycans can act as recognition signals for various cellular receptors, influencing cellular signaling pathways.
* **Immune recognition:** O-linked glycosylation patterns on proteins can influence immune responses, affecting the interaction with immune cells.

Overall, O-linked glycosylation via threonine is a complex and essential process that adds significant diversity and functionality to proteins, impacting a wide range of biological activities.'
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Proteins (5)

Compounds (6)