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Chemical biology tools to interrogate the roles of O-GlcNAc in immunity
The O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation of proteins is an essential and dynamic post-translational modification in mammalian cells that is regulated by the action of two enzymes. O-GlcNAc transferase (OGT) incorporates this monosaccharide on serine/threonine residues, whereas O-G...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2023
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9910173/ https://www.ncbi.nlm.nih.gov/pubmed/36776401 http://dx.doi.org/10.3389/fimmu.2022.1089824 |
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author | Saha, Abhijit Fernández-Tejada, Alberto |
author_facet | Saha, Abhijit Fernández-Tejada, Alberto |
author_sort | Saha, Abhijit |
collection | PubMed |
description | The O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation of proteins is an essential and dynamic post-translational modification in mammalian cells that is regulated by the action of two enzymes. O-GlcNAc transferase (OGT) incorporates this monosaccharide on serine/threonine residues, whereas O-GlcNAcase (OGA) removes it. This modification is found on thousands of intracellular proteins involved in vital cellular processes, both under physiological and pathological conditions. Aberrant expression of O-GlcNAc has been implicated in diseases such as Alzheimer, diabetes, and cancer, and growing evidence over the last decade has also revealed key implications of O-GlcNAcylation in immunity. While some key signaling pathways involving O-GlcNAcylation in immune cells have been discovered, a complete mechanistic understanding of how O-GlcNAcylated proteins function in the immune system remains elusive, partly because of the difficulties in mapping and quantifying O-GlcNAc sites. In this minireview, we discuss recent progress on chemical biology tools and approaches to investigate the role of O-GlcNAcylation in immune cells, with the intention of encouraging further research and developments in chemical glycoimmunology that can advance our understanding of O-GlcNAc in immunity. |
format | Online Article Text |
id | pubmed-9910173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-99101732023-02-10 Chemical biology tools to interrogate the roles of O-GlcNAc in immunity Saha, Abhijit Fernández-Tejada, Alberto Front Immunol Immunology The O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation of proteins is an essential and dynamic post-translational modification in mammalian cells that is regulated by the action of two enzymes. O-GlcNAc transferase (OGT) incorporates this monosaccharide on serine/threonine residues, whereas O-GlcNAcase (OGA) removes it. This modification is found on thousands of intracellular proteins involved in vital cellular processes, both under physiological and pathological conditions. Aberrant expression of O-GlcNAc has been implicated in diseases such as Alzheimer, diabetes, and cancer, and growing evidence over the last decade has also revealed key implications of O-GlcNAcylation in immunity. While some key signaling pathways involving O-GlcNAcylation in immune cells have been discovered, a complete mechanistic understanding of how O-GlcNAcylated proteins function in the immune system remains elusive, partly because of the difficulties in mapping and quantifying O-GlcNAc sites. In this minireview, we discuss recent progress on chemical biology tools and approaches to investigate the role of O-GlcNAcylation in immune cells, with the intention of encouraging further research and developments in chemical glycoimmunology that can advance our understanding of O-GlcNAc in immunity. Frontiers Media S.A. 2023-01-26 /pmc/articles/PMC9910173/ /pubmed/36776401 http://dx.doi.org/10.3389/fimmu.2022.1089824 Text en Copyright © 2023 Saha and Fernández-Tejada https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Immunology Saha, Abhijit Fernández-Tejada, Alberto Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title | Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title_full | Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title_fullStr | Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title_full_unstemmed | Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title_short | Chemical biology tools to interrogate the roles of O-GlcNAc in immunity |
title_sort | chemical biology tools to interrogate the roles of o-glcnac in immunity |
topic | Immunology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9910173/ https://www.ncbi.nlm.nih.gov/pubmed/36776401 http://dx.doi.org/10.3389/fimmu.2022.1089824 |
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