AI Article Synopsis
- - O-linked β-N-acetylglucosamine (O-GlcNAc) is an important form of glycosylation found in many organisms, crucial for proper cellular function and linked to diseases like cancer and metabolic syndrome.
- - The study focuses on how O-GlcNAcylation affects the COPII complex, which is vital for transporting proteins from the endoplasmic reticulum in cells.
- - Researchers discovered new O-GlcNAcylation sites on key COPII proteins and suggest that this glycosylation may be influenced by nutrient levels, linking metabolism with protein trafficking in cells.
Article Abstract
O-linked β-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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8457363 | PMC |
| http://dx.doi.org/10.1093/glycob/cwab055 | DOI Listing |
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