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Glycobiology ; 31(9): 1102-1120, 2021 09 20.
Article in English | MEDLINE | ID: mdl-34142147

ABSTRACT

O-linked ß-N-acetylglucosamine (O-GlcNAc) is a dynamic form of intracellular glycosylation common in animals, plants and other organisms. O-GlcNAcylation is essential in mammalian cells and is dysregulated in myriad human diseases, such as cancer, neurodegeneration and metabolic syndrome. Despite this pathophysiological significance, key aspects of O-GlcNAc signaling remain incompletely understood, including its impact on fundamental cell biological processes. Here, we investigate the role of O-GlcNAcylation in the coat protein II complex (COPII), a system universally conserved in eukaryotes that mediates anterograde vesicle trafficking from the endoplasmic reticulum. We identify new O-GlcNAcylation sites on Sec24C, Sec24D and Sec31A, core components of the COPII system, and provide evidence for potential nutrient-sensitive pathway regulation through site-specific glycosylation. Our work suggests a new connection between metabolism and trafficking through the conduit of COPII protein O-GlcNAcylation.


Subject(s)
Acetylglucosamine , Endoplasmic Reticulum , Acetylglucosamine/metabolism , Animals , Endoplasmic Reticulum/metabolism , Glycosylation , Mammals/metabolism , N-Acetylglucosaminyltransferases/metabolism , Nutrients , Protein Processing, Post-Translational , Signal Transduction
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