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.