protein O-linked glycosylation via serine

Definition

Target type: biologicalprocess

The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine. [RESID:AA0154]

O-linked glycosylation via serine is a crucial post-translational modification that adds sugar moieties to the hydroxyl group of serine residues within a protein. This process is facilitated by a family of enzymes known as glycosyltransferases, which specifically recognize and attach specific sugar molecules to the serine residue. The glycosylation process typically begins with the transfer of an N-acetylglucosamine (GlcNAc) sugar residue from a donor molecule, UDP-GlcNAc, to the hydroxyl group of serine. This initial step is catalyzed by an enzyme called O-GlcNAc transferase (OGT). Once the initial GlcNAc residue is attached, further modifications can occur, such as the addition of other sugars like galactose, fucose, or sialic acid. These modifications are catalyzed by specific glycosyltransferases that exhibit substrate specificity for both the protein and the sugar being added. O-linked glycosylation via serine plays a significant role in various cellular processes, including protein folding, trafficking, stability, and signaling. It can influence protein-protein interactions, modulate enzyme activity, and impact cellular localization. The specific function of O-linked glycosylation depends on the protein's structure, the site of glycosylation, and the nature of the attached sugar moieties. Disruptions in O-linked glycosylation have been implicated in various diseases, highlighting the importance of this process for normal cellular function.'
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Proteins (4)

Compounds (6)