N-glycan fucosylation

Definition

Target type: biologicalprocess

The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains. [GOC:sart, PMID:19948734]

N-glycan fucosylation is a crucial post-translational modification that adds a fucose sugar residue to the core structure of N-linked glycans. This process occurs in the Golgi apparatus of eukaryotic cells and plays a critical role in various biological functions, including protein folding, trafficking, and cell-cell interactions.

The fucosylation process begins with the activation of GDP-fucose, a sugar nucleotide precursor, by the enzyme GDP-fucose synthase. This activated form of fucose is then transferred to the N-glycan by a specific glycosyltransferase called fucosyltransferase. There are multiple fucosyltransferases with varying substrate specificities, leading to the formation of different fucosylated glycan structures.

One of the most common types of N-glycan fucosylation is the α1,6-fucosylation, where fucose is linked to the N-acetylglucosamine (GlcNAc) residue at the reducing end of the core N-glycan. This modification, often referred to as the "core fucosylation," is catalyzed by the enzyme α1,6-fucosyltransferase (FUT8).

Fucosylation can also occur at other positions within the N-glycan, such as the α1,3-fucosylation, where fucose is attached to the first GlcNAc residue of the core N-glycan. This type of fucosylation is catalyzed by the enzyme α1,3-fucosyltransferase (FUT9).

The specific type of fucosylation and the location of the fucose residue on the N-glycan can significantly influence the biological function of the modified protein. For instance, core fucosylation has been implicated in modulating protein folding, stability, and interactions with lectins. It can also influence the trafficking and secretion of proteins.

In addition to its role in protein function, N-glycan fucosylation has also been linked to various biological processes, including immune responses, cell signaling, and development. For example, fucosylation of glycoproteins can influence their recognition by immune cells, playing a role in antibody-mediated immunity.

Overall, N-glycan fucosylation is a complex and highly regulated process with diverse biological implications. Understanding the mechanisms and functions of fucosylation is essential for comprehending the intricate roles of glycoproteins in cellular processes and human health.'
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Proteins (2)

Compounds (12)