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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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Autores principales: Saha, Abhijit, Fernández-Tejada, Alberto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2023
Materias:
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.
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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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