Oglcnacylation

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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. A better understanding of the roles of O -GlcNAcylation in physiopathological processes would help to uncover novel avenues for therapeutic intervention. The aim of this review is to discuss the recent updates on the mechanisms and impacts of O -GlcNAcylation on these diseases, and its potential as a new clinical target.

Oglcnacylation

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. This protein modification interacts with key cellular pathways involved in transcription, translation, and proteostasis. Although ubiquitous throughout the body, O-GlcNAc is particularly abundant in the brain, and various proteins commonly found at synapses are O-GlcNAcylated. Recent studies have demonstrated that the modulation of O-GlcNAc in the brain alters synaptic and neuronal functions. Furthermore, altered brain O-GlcNAcylation is associated with either the etiology or pathology of numerous neurodegenerative diseases, while the manipulation of O-GlcNAc exerts neuroprotective effects against these diseases. Although the detailed molecular mechanisms underlying the functional roles of O-GlcNAcylation in the brain remain unclear, O-GlcNAcylation is critical for regulating diverse neural functions, and its levels change during normal and pathological aging. In this review, we will highlight the functional importance of O-GlcNAcylation in the brain and neurodegenerative diseases. Dario F. O-GlcNAcylation occurs in various cellular locations, such as the nucleus, cytosol, and cellular organelles, including mitochondria, the cytoskeleton, and the endoplasmic reticulum Hence, it is conceivable that O-GlcNAcylation, through its competitive interplay with phosphorylation, could critically affect a variety of cellular signaling pathways by dynamically modulating protein activities 8 , O-GlcNAcylation is a posttranslational modification that attaches O-GlcNAc moieties to serine or threonine residues of cellular proteins. O-GlcNAcylation can regulate important cellular processes such as gene expression, signal transduction, cell cycle, nutrient sensing, protein homeostasis, cellular stress response, and neuronal function.

Radiolabeled [ 3 H]galactose shown in red.

Journal of Biomedical Science volume 27 , Article number: 57 Cite this article. Metrics details. O -GlcNAcylation couples the processes of nutrient sensing, metabolism, signal transduction and transcription, and plays important roles in development, normal physiology and physiopathology. Particularly, O -GlcNAcylation has been shown to have intricate crosstalk with phosphorylation as they both modify serine or threonine residues. Aberrant O -GlcNAcylation on various protein substrates has been implicated in many diseases, including neurodegenerative diseases, diabetes and cancers.

O-GlcNAcylation is an atypical, reversible, and dynamic glycosylation that plays a critical role in maintaining the normal physiological functions of cells by regulating various biological processes such as signal transduction, proteasome activity, apoptosis, autophagy, transcription, and translation. It can also respond to environmental changes and physiological signals to play the role of "stress receptor" and "nutrition sensor" in a variety of stress responses and biological processes. Even, a homeostatic disorder of O-GlcNAcylation may cause many diseases. Therefore, O-GlcNAcylation and its regulatory role in stress response are reviewed in this paper. Abstract O-GlcNAcylation is an atypical, reversible, and dynamic glycosylation that plays a critical role in maintaining the normal physiological functions of cells by regulating various biological processes such as signal transduction, proteasome activity, apoptosis, autophagy, transcription, and translation. Publication types Research Support, Non-U. Gov't Review. Substances Proteins.

Oglcnacylation

Molecular Medicine volume 28 , Article number: Cite this article. Metrics details. In eukaryotes, only two conserved enzymes are involved in this process. Aberrant O -GlcNAcylation is associated with a variety of human diseases, such as diabetes, cancer, neurodegenerative diseases, and cardiovascular diseases. Numerous studies have confirmed that O -GlcNAcylation is involved in the occurrence and progression of cancers in multiple systems throughout the body.

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Circulation , — Ten-eleven translocation 1 Tet1 is regulated by O -linked N -acetylglucosamine transferase Ogt for target gene repression in mouse embryonic stem cells. What is type 2 diabetes? In addition to substrate recognition by TPRs, interaction between the OGT catalytic cleft and the acceptor peptide is also pivotal for OGT to select its substrates [ 45 , 46 ]. O-GlcNAc transferase promotes fatty liver-associated liver cancer through inducing palmitic acid and activating endoplasmic reticulum stress. Synergy of peptide and sugar in O -GlcNAcase substrate recognition. Davie, C. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. In contrast, selective enhancement of O-GlcNAcylation in dopamine neurons did not negatively impact neuronal structures or survival. Ferrer, C. O-GlcNAc and the cardiovascular system. Banerjee, P. White MF.

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Microglia is the brain resident macrophage [ 88 ]. Considering the crosstalk with phosphorylation, O-GlcNAcylation may suppress excessive phosphorylation of neurofilaments and concomitantly alleviate ALS pathology. One of the major features of T2D is insulin resistance, defined as the inability of insulin to trigger appropriate glucose uptake Carpenter et al. Various cellular stress stimuli have been associated with changes in O -GlcNAc. Starvation, stress resistance, and cancer. Neuronal O-GlcNAcylation improves cognitive function in the aged mouse brain. Neuron 39 , — Its nuclear accumulation in response to gene mutations is directly linked to the onset of typical cancers, through which it regulates cell proliferation and metastasis Cui et al. CA Cancer J Clin. Trapannone, R.