Core fucosylation and its roles in gastrointestinal glycoimmunology

Abstract

Glycosylation is a common post-translational modification in eukaryotic cells. It is involved in the production of many biologically active glycoproteins and the regulation of protein structure and function. Core fucosylation plays a vital role in the immune response. Most immune system molecules are core fucosylated glycoproteins such as complements, cluster differentiation antigens, immunoglobulins, cytokines, major histocompatibility complex molecules, adhesion molecules, and immune molecule synthesis-related transcription factors. These core fucosylated glycoproteins play important roles in antigen recognition and clearance, cell adhesion, lymphocyte activation, apoptosis, signal transduction, and endocytosis. Core fucosylation is dominated by fucosyltransferase 8 (Fut8), which catalyzes the addition of α-1,6-fucose to the innermost GlcNAc residue of N-glycans. Fut8 is involved in humoral, cellular, and mucosal immunity. Tumor immunology is associated with aberrant core fucosylation. Here, we summarize the roles and potential modulatory mechanisms of Fut8 in various immune processes of the gastrointestinal system.

Keywords: Fucosyltransferase 8; Core fucosylation; Glycoimmunology; Gastrointestinal tumor immunology; T cell signal pathway

Core Tip: Core fucosylation is driven by fucosyltransferase 8 (Fut8), which catalyzes the addition of α-1,6-fucose to the innermost GlcNAc residue of N-glycans. Core fucosylation plays a vital role in immune responses. Most immune system molecules are core fucosylated glycoproteins that play important roles in antigen recognition and clearance, cell adhesion, lymphocyte activation, apoptosis, signal transduction, and endocytosis. Fut8 is involved in humoral immune responses, cellular immunity, mucosal immunity, and tumor immunology. Here, we summarize the roles and potential modulatory mechanisms of Fut8 in various immune responses of the gastrointestinal system.