Protein O-glycosylation regulates diverse developmental and defense processes in plants

Post-translational modifications affect protein functions and play key roles in controlling biological processes. Plants have unique types of O-glycosylation that are different from those of animals and prokaryotes, and they play roles in modulating the functions of secretory proteins and nucleocytoplasmic proteins by regulating transcription and mediating localization and degradation. O-glycosylation is complex because of the dozens of different O-glycan types, the widespread existence of hydroxyproline (Hyp), serine (Ser), and threonine (Thr) residues in proteins attached by O-glycans, and the variable modes of linkages connecting the sugars. O-glycosylation specifically affects development and environmental acclimatization by affecting diverse physiological processes. This review describes recent studies on the detection and functioning of protein O-glycosylation in plants, and provides a framework for the O-glycosylation network that underlies plant development and resistance. O-glycosylation of polypeptides including Hyp-O-glycosylation, O-GlcNAcylation, and O-fucosylation play key roles in molecular mechanisms that control diverse developmental and defense processes in plants.

Automated summary

Post-translational modifications have significant effects on protein functions, with O-glycosylation playing a crucial role in controlling biological processes in plants. Plants have unique types of O-glycosylation, different from animals and prokaryotes, that regulate transcription, localization, and protein degradation. O-glycosylation is complex due to the various types of O-glycan, prevalence of Hyp, Ser, and Thr residues, and variable sugar linkages. It specifically affects development and environmental acclimatization in diverse physiological processes.