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N -glycosylation is an essential protein modification that plays roles in many diverse biological processes including protein folding, quality control and protein interactions. Despite recent advances in characterization of the  N -glycosylation and  N -glycan processing machinery our understanding of  N -glycosylation related processes in plant development is limited. In  Arabidopsis thaliana , failure of mannose trimming from oligomannosidic  N -glycans in the endoplasmic reticulum (ER) and  cis /medial-Golgi leads to a defect in root development in the  mns123  triple mutant. Here, we show that the severe root phenotype of  mns123  is restored in asparagine-linked glycosylation (ALG)-deficient plants with distinct defects in the biosynthesis of the lipid-linked oligosaccharide precursor. The root growth of these ALG-deficient plants is not affected by the α-mannosidase inhibitor kifunensine. Genetic evidence shows that the defect is uncoupled from the glycan-dependent ER-associated degradation (ERAD) pathway that removes misfolded glycoproteins with oligomannosidic  N -glycans from the ER. Restoration of mannose trimming using a  trans -Golgi targeted α-mannosidase suppresses the defect of  mns123  roots. These data suggest that processing of terminal mannose residues from oligomannosidic  N -glycans is important for an unknown late-Golgi or post-Golgi process that is implicated in proper root formation.

Processing of the Terminal Alpha-1,2-Linked Mannose Residues From Oligomannosidic N-Glycans Is Critical for Proper Root Growth