The Roles of the N-terminal α-helical and C-terminal Src Homology 3 Domains in the Enzymatic Functions of FUT8

The core alpha 1,6-fucose structure, a major structure in asparagine-linked oligosaccharides, has a variety of biological and physiological characteristics. In eukaryotes, the core alpha 1,6-fucose structure is biosynthesized by the alpha 1,6-fticosyltransferase, FUT8. FUT8 is composed of a catalytic domain and two additional domains, an N-terminal alpha-helical (coiled-coil) and a C-terminal Src homology 3 (SH3) domain. The most recent structural and biochemical studies clearly show that these domains have precise functions. In this minireview, we summarize our current knowledge of the roles of the alpha-helical (coiled-coil) and SH3 domains in FUT8 functions, with a particular focus on the dimer formation that is essential for the activity, substrate recognition and other characteristics of this enzyme.

Automated summary

This review summarizes the biological and physiological characteristics of the core alpha 1,6-fucose structure in asparagine-linked oligosaccharides, with a focus on the importance of the alpha-helical (coiled-coil) and SH3 domains in the function of FUT8 enzyme. The formation of dimers is crucial for the activity, substrate recognition, and other characteristics of this enzyme.