Oglcnacylation

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These enzymes are found ubiquitously in eukaryotes and genetic knock outs of the ogt gene has been found to be lethal in embryonic mice. The substrate scope of these enzymes is vast, over 15, proteins across 43 species have been identified with O -GlcNAc. OGN has been known to play a key role in several cellular processes such as: transcription, translation, cell signaling, nutrient sensing, immune cell development and various steps of the cell cycle. However, its dysregulation is present in various diseases: cancer, neurodegenerative diseases, diabetes. This crosstalk between PTMs can affect gene expression, protein localization, and protein stability; therefore, regulating a multitude of cell signaling pathways. In this review the roles of OGN will be discussed.

Oglcnacylation

O -GlcNAc differs from other forms of protein glycosylation : i O -GlcNAc is not elongated or modified to form more complex glycan structures, ii O -GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins , and iii O -GlcNAc is a highly dynamic modification that turns over more rapidly than the proteins which it modifies. O -GlcNAc is conserved across metazoans. Due to the dynamic nature of O -GlcNAc and its presence on serine and threonine residues, O -GlcNAcylation is similar to protein phosphorylation in some respects. First reported in , this post-translational modification has since been identified on over 5, proteins. In , the Hart lab was probing for terminal GlcNAc residues on the surfaces of thymocytes and lymphocytes. O -GlcNAc is generally a dynamic modification that can be cycled on and off various proteins. Some residues are thought to be constitutively modified by O -GlcNAc. Consequently, predicting sites of O -GlcNAc modification is challenging, and identifying modification sites generally requires mass spectrometry methods. For OGT, studies have shown that substrate recognition is regulated by a number of factors including aspartate [19] and asparagine [20] ladder motifs in the lumen of the superhelical TPR domain, active site residues, [21] and adaptor proteins. Several methods exist to detect the presence of O -GlcNAc and characterize the specific residues modified. Wheat germ agglutinin , a plant lectin , is able to recognize terminal GlcNAc residues and is thus often used for detection of O -GlcNAc. This lectin has been applied in lectin affinity chromatography for the enrichment and detection of O -GlcNAc.

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Federal government websites often end in. The site is secure. O -linked N -acetylglucosamine O -GlcNAc is a dynamic post-translational modification occurring on myriad proteins in the cell nucleus, cytoplasm, and mitochondria. O -GlcNAcylation is involved in a number of important cell processes including transcription, translation, metabolism, signal transduction, and apoptosis. Deregulation of O -GlcNAcylation has been reported to be associated with various human diseases such as cancer, diabetes, neurodegenerative diseases, and cardiovascular diseases.

Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. O -GlcNAcylation is a post-translational modification of protein in response to genetic variations or environmental factors, which is controlled by two highly conserved enzymes, i.

Oglcnacylation

This modification impacts protein functionality, influencing stability, protein-protein interactions, and localization. Its interaction with other modifications such as phosphorylation and ubiquitination is becoming increasingly evident. Dysregulation of O-GlcNAcylation is associated with numerous human diseases, including diabetes, nervous system degeneration, and cancers. This review extensively explores the regulatory mechanisms of O-GlcNAcylation, its effects on cellular physiology, and its role in the pathogenesis of diseases. It examines the implications of aberrant O-GlcNAcylation in diabetes and tumorigenesis, highlighting novel insights into its potential role in cardiovascular diseases.

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Vella, P. Elsen, N. Qian, K. The preferential utilization of glycolysis and lactic acid fermentation for ATP production despite the availability of oxygen for oxidative phosphorylation; it is a hallmark of metabolic reprogramming in cancer. Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. A survival response of mammalian cells. Cell , — Xu, S. What is type 2 diabetes? Dong, D. Insulin signaling controls the expression of O -GlcNAc transferase and its interaction with lipid microdomains. Morgan, S. Hyper-O-GlcNAcylation activates nuclear factor kappa-light-chain-enhancer of activated B cells NF-kappaB signaling through interplay with phosphorylation and acetylation. Kalia, L.

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These hydrophobic interactions are important for spatial constraints and protein binding; consistently, mutation of these residues causes reduced binding of human OGA to the substrates [ 50 ]. However, one major question that needs to be resolved in future studies is whether O -GlcNAcylation causes diabetes or is just an effect of the overall dysfunction seen in this disease. Olszewski, N. The formation of the final product in this pathway, alpha uridine diphosphate-N-acetylglucosamine UDP-GlcNAc , combines to monitor the metabolism of glucose, amino acids, fatty acids, and nucleotides. Glycobiology 17 , — Oga-1 and ogt-1 knockout nematodes display similar, but not contrary, phenotype in insulin-like signaling [ , ], suggesting that OGT and OGA seem to coordinately regulate the level of intracellular O -GlcNAcylation. Cancer Lett. J Neurol Sci. O-GlcNAc transferase regulates excitatory synapse maturity. Most importantly, accumulating studies have demonstrated that genetic or pharmacological manipulation of O-GlcNAcylation remarkably alters neuronal and synaptic functions in the brain.