O-GlcNAcylation of Thr¹²/Ser⁵⁶ in short-form O-GlcNAc transferase (sOGT) regulates its substrate selectivity.

ABSTRACT: O-GlcNAcylation is a ubiquitous protein glycosylation playing different roles on variant proteins. O-GlcNAc transferase (OGT) is the unique enzyme responsible for the sugar addition to nucleocytoplasmic proteins. Recently, multiple O-GlcNAc sites have been observed on short-form OGT (sOGT) and nucleocytoplasmic OGT (ncOGT), both of which locate in the nucleus and cytoplasm in cell. Moreover, O-GlcNAcylation of Ser³⁸⁹ in ncOGT (1036 amino acids) affects its nuclear translocation in HeLa cells. To date, the major O-GlcNAcylation sites and their roles in sOGT remain unknown. Here, we performed LC-MS/MS and mutational analyses to seek the major O-GlcNAcylation site on sOGT. We identified six O-GlcNAc sites in the tetratricopeptide rep

SUBMITTER: Liu L 

PROVIDER: S-EPMC6851338 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature