GONST2 transports GDP-Mannose for sphingolipid glycosylation in the Golgi apparatus of Arabidopsis

<jats:title>Abstract</jats:title><jats:p>The Golgi lumen is the site of many different glycosylation events, including cell wall polysaccharide biosynthesis and lipid glycosylation. Transporters are necessary for the import of the substrates required for glycosylation (nucleotide sugars) from the cytosol where they are synthesized. Plants use four GDP-linked sugars to glycosylate macromolecules: GDP-L-Fucose, GDP-D-Mannose, GDP-L-Galactose and GDP-D-Glucose. Of the predicted fifty-one members of the nucleotide sugar transporter/triose phosphate transporter family in Arabidopsis, only four appear to contain the conserved motif needed for the transport of GDP-linked sugars, GOLGI LOCALIZED NUCLEOTIDE SUGAR TRANSPORTER (GONST) 1-4. Previously, we have demonstrated that GONST1 provides GDP-D-Mannose for glycosylation of a class of sphingolipids, the glycosylinositolphosphorylceramides (GIPCs). Here, we characterize its closest homologue, GONST2, and conclude that it also specifically provides substrate for GIPC glycosylation. Expression of<jats:italic>GONST2</jats:italic>driven by the<jats:italic>GONST1</jats:italic>promoter is able to rescue the severe growth phenotype of<jats:italic>gonst1</jats:italic>. Loss of GONST2 exacerbates the<jats:italic>gonst1</jats:italic>constitutive hypersensitive response, as well as the reduced cell wall cellulose content. The<jats:italic>gonst2</jats:italic>mutant grows normally under standard conditions, but has enhanced resistance to the powdery mildew-causing fungus<jats:italic>Golovinomyces orontii</jats:italic>.</jats:p>