Oglcnacylation

O -GlcNAc differs from other oglcnacylation of protein glycosylation : i O -GlcNAc is not elongated or modified to form more complex glycan oglcnacylation, ii O -GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteinsoglcnacylation, 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 oglcnacylation, O -GlcNAcylation is similar to protein phosphorylation in some respects, oglcnacylation.

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.

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 ,

It is expected that there will be an increasing number of oglcnacylation driven to establish a set of simpler and more reliable O -GlcNAc detection methods. Together, oglcnacylation, these studies indicate a critical role of O-GlcNAcylation in modulating ALS pathology oglcnacylation inhibiting excessive oglcnacylation and protein aggregation and reducing ROS accumulation. Femiclear and perspectives O-GlcNAcylation critically contributes to various cellular processes, including transcription, oglcnacylation, translation, signaling cascades, and protein homeostasis, in a multitude of cell types, and more than human proteins have been identified as O-GlcNAcylated proteins thus far

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.

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. The review also discusses the interplay of O-GlcNAcylation with other protein modifications and its impact on cell growth and metabolism. By synthesizing current research, this review elucidates the multifaceted roles of O-GlcNAcylation, providing a comprehensive reference for future studies. It underscores the potential of targeting the O-GlcNAcylation cycle in developing novel therapeutic strategies for various pathologies. Publication types Review.

Oglcnacylation

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.

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Thus, another possibility is that both hyper- and hypo- O -GlcNAcylation may cause immune deregulation. J Biol Chem 38 — Consent for publication Not applicable. Br J Pharmacol. Ma, X. Probing the dynamics of O -GlcNAc glycosylation in the brain using quantitative proteomics. You can also search for this author in PubMed Google Scholar. Zeng, Q. FOXOs: signalling integrators for homeostasis maintenance. Cell Chemical Biology. Here we provide a brief summary on how this post-translational modification functions as a critical factor involving physiological and pathological processes. Pre-initiation complex A large protein assembly that performs various functions that are required for transcription initiation for example, the recruitment of RNA polymerase II to transcription start sites and the unwinding of DNA to allow for RNA polymerase II binding.

Journal of Biomedical Science volume 27 , Article number: 57 Cite this article.

Zhao, M. Cell 6 — Science —9. Nat Chem Biol. Alonso, J. This inhibitory form is referred to as reciprocal crosstalk. Dynamic interplay between O-glycosylation and O-phosphorylation of nucleocytoplasmic proteins: a new paradigm for metabolic control of signal transduction and transcription. Mol Cell 1 5 — O-GlcNAcylation in Cancer biology: linking metabolism and signaling. Although a chemoenzymatic labelling approach had been available Yi et al. BMC Biol. In HD mouse models, distortion of the nuclear membrane and disrupted nucleocytoplasmic transport were also observed