Plant Fucosyltransferases and the Emerging Biological Importance of Fucosylated Plant Structures

Abstract

Plants frequently incorporate the monosaccharide L-fucose (Fuc; 6-deoxy-Lgalactose) into glycans and glycopolymers located in diverse cellular locations. The incorporation of Fuc onto these varied glycans is carried out by fucosyltransferases (FUTs), that make up a protein superfamily with equally varied and diverse functions. The structures wherein Fuc is found have numerous proposed and validated functions, ranging from plant growth and development, cell expansion, adhesion and signaling, to energy metabolism, among others. FUTs from several different plant species have been identified and described; however, very few of them have been extensively characterized biochemically and biologically. In this review, we summarize plant FUTs that have been biochemically characterized and biologically investigated for associated phenotypes, offering greater insight and understanding into the physiological importance of Fuc in plants and in plant cell wall structures, glycans, and proteins.

Ancient origin of fucosylated xyloglucan in charophycean green algae

“…However, synthesis of fucosylated XyG has been demonstrated in pollen tubes of tobacco 58 , also belonging to Solanaceae, corroborating that fucosylation was not acquired multiple times during evolution but rather lost in tissues where no selection pressure favors its conservation. It appears that fucosylated XyG has functional properties that sets it apart from XyG in general 65 but it is not yet clear what precisely is the decisive property.…”

Golgi fucosyltransferase 1 reveals its important role in α-1,4-fucose modification of N-glycan in CRISPR/Cas9 diatom Phaeodactylum tricornutum

“…In recent years, several studies investigated the types, subcellular localization, and functions of fucosyltransferase (FucT) in different eukaryotes, including animals and plants [ 6 ]. Fucosyltransferase is responsible for the transfer of fucose residue from GDP-fucose to the N-glycan of neosynthesized glycoproteins during the N-glycosylation.…”

AtFUT4 and AtFUT6 Are Arabinofuranose-Specific Fucosyltransferases

“…FUTs are glycosyltransferases (GTs) that catalyze the transfer of Fuc from guanidine 5'-diphosphate-β- l -fucose (GDP-Fuc) onto a suitable acceptor substrate, typically a glycan or protein. Although largely understudied in plants, known and putative FUTs are highly prevalent in many plant genomes ( Soto et al, 2019 ). Interestingly, unlike the FUTs found in vertebrates and invertebrates that form clades based on predicted function ( Martinez-Duncker et al, 2003 ), the FUTs in plants form terminal clades largely composed of single or closely related species ( Soto et al, 2019 ).…”

“…Although largely understudied in plants, known and putative FUTs are highly prevalent in many plant genomes ( Soto et al, 2019 ). Interestingly, unlike the FUTs found in vertebrates and invertebrates that form clades based on predicted function ( Martinez-Duncker et al, 2003 ), the FUTs in plants form terminal clades largely composed of single or closely related species ( Soto et al, 2019 ). The model plant species Arabidopsis thaliana has 13 FUTs, 10 of which are classified as members of GT family 37 (GT37) according to the Carbohydrate-Active enZYmes (CAZy) database, and they are all predicted to be Golgi-localized type-II transmembrane proteins ( Sarria et al, 2001 ; Lombard et al, 2014 ).…”