Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease

O-GlcNAc is a pleotropic, enigmatic post-translational modification (PTM). This PTM modifies thousands of proteins differentially across tissue types and regulates diverse cellular signaling processes. O-GlcNAc is implicated in numerous diseases, and the advent of O-GlcNAc perturbation as a novel cl...

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Detalles Bibliográficos
Autores principales: Burt, Rajan A., Alghusen, Ibtihal M., John Ephrame, Sophiya, Villar, Maria T., Artigues, Antonio, Slawson, Chad
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Molecular Biosciences
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9161079/
https://www.ncbi.nlm.nih.gov/pubmed/35664676
http://dx.doi.org/10.3389/fmolb.2022.920727
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author Burt, Rajan A.
Alghusen, Ibtihal M.
John Ephrame, Sophiya
Villar, Maria T.
Artigues, Antonio
Slawson, Chad
author_facet Burt, Rajan A.
Alghusen, Ibtihal M.
John Ephrame, Sophiya
Villar, Maria T.
Artigues, Antonio
Slawson, Chad
author_sort Burt, Rajan A.
collection PubMed
description O-GlcNAc is a pleotropic, enigmatic post-translational modification (PTM). This PTM modifies thousands of proteins differentially across tissue types and regulates diverse cellular signaling processes. O-GlcNAc is implicated in numerous diseases, and the advent of O-GlcNAc perturbation as a novel class of therapeutic underscores the importance of identifying and quantifying the O-GlcNAc modified proteome. Here, we review recent advances in mass spectrometry-based proteomics that will be critical in elucidating the role of this unique glycosylation system in health and disease.
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spelling pubmed-91610792022-06-03 Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease Burt, Rajan A. Alghusen, Ibtihal M. John Ephrame, Sophiya Villar, Maria T. Artigues, Antonio Slawson, Chad Front Mol Biosci Molecular Biosciences O-GlcNAc is a pleotropic, enigmatic post-translational modification (PTM). This PTM modifies thousands of proteins differentially across tissue types and regulates diverse cellular signaling processes. O-GlcNAc is implicated in numerous diseases, and the advent of O-GlcNAc perturbation as a novel class of therapeutic underscores the importance of identifying and quantifying the O-GlcNAc modified proteome. Here, we review recent advances in mass spectrometry-based proteomics that will be critical in elucidating the role of this unique glycosylation system in health and disease. Frontiers Media S.A. 2022-05-19 /pmc/articles/PMC9161079/ /pubmed/35664676 http://dx.doi.org/10.3389/fmolb.2022.920727 Text en Copyright © 2022 Burt, Alghusen, John Ephrame, Villar, Artigues and Slawson. 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 Molecular Biosciences
Burt, Rajan A.
Alghusen, Ibtihal M.
John Ephrame, Sophiya
Villar, Maria T.
Artigues, Antonio
Slawson, Chad
Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title_full Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title_fullStr Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title_full_unstemmed Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title_short Mapping the O-GlcNAc Modified Proteome: Applications for Health and Disease
title_sort mapping the o-glcnac modified proteome: applications for health and disease
topic Molecular Biosciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9161079/
https://www.ncbi.nlm.nih.gov/pubmed/35664676
http://dx.doi.org/10.3389/fmolb.2022.920727
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