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O-GlcNAc profiling: from proteins to proteomes

O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and s...

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Detalles Bibliográficos
Autores principales: Ma, Junfeng, Hart, Gerald W
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4015695/
https://www.ncbi.nlm.nih.gov/pubmed/24593906
http://dx.doi.org/10.1186/1559-0275-11-8
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author Ma, Junfeng
Hart, Gerald W
author_facet Ma, Junfeng
Hart, Gerald W
author_sort Ma, Junfeng
collection PubMed
description O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and signal transduction. Aberrant protein O-GlcNAcylation is directly linked to the pathological progression of chronic diseases including diabetes, cancer, and neurodegenerative disorders. Identification, site mapping, and quantification of O-GlcNAc proteins are a prerequisite to decipher their functions. In this review, we mainly focus on technological developments regarding O-GlcNAc protein profiling. Specifically, on one hand, we show how these techniques are being used for the comprehensive characterization of certain targeted proteins in which biologists are most interested. On the other hand, we present several newly developed approaches for O-GlcNAcomic profiling as well as how they provide us with a systems perspective to crosstalk amongst different PTMs and complicated biological events. Promising technical trends are also highlighted to evoke more efforts by diverse laboratories, which would further expand our understanding of the physiological and pathological roles of protein O-GlcNAcylation in chronic diseases.
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spelling pubmed-40156952014-05-23 O-GlcNAc profiling: from proteins to proteomes Ma, Junfeng Hart, Gerald W Clin Proteomics Review O-linked β-D-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) onto serine and threonine residues of proteins is an important post-translational modification (PTM), which is involved in many crucial biological processes including transcription, translation, proteasomal degradation, and signal transduction. Aberrant protein O-GlcNAcylation is directly linked to the pathological progression of chronic diseases including diabetes, cancer, and neurodegenerative disorders. Identification, site mapping, and quantification of O-GlcNAc proteins are a prerequisite to decipher their functions. In this review, we mainly focus on technological developments regarding O-GlcNAc protein profiling. Specifically, on one hand, we show how these techniques are being used for the comprehensive characterization of certain targeted proteins in which biologists are most interested. On the other hand, we present several newly developed approaches for O-GlcNAcomic profiling as well as how they provide us with a systems perspective to crosstalk amongst different PTMs and complicated biological events. Promising technical trends are also highlighted to evoke more efforts by diverse laboratories, which would further expand our understanding of the physiological and pathological roles of protein O-GlcNAcylation in chronic diseases. Springer 2014-03-05 /pmc/articles/PMC4015695/ /pubmed/24593906 http://dx.doi.org/10.1186/1559-0275-11-8 Text en Copyright © 2014 Ma and Hart; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Ma, Junfeng
Hart, Gerald W
O-GlcNAc profiling: from proteins to proteomes
title O-GlcNAc profiling: from proteins to proteomes
title_full O-GlcNAc profiling: from proteins to proteomes
title_fullStr O-GlcNAc profiling: from proteins to proteomes
title_full_unstemmed O-GlcNAc profiling: from proteins to proteomes
title_short O-GlcNAc profiling: from proteins to proteomes
title_sort o-glcnac profiling: from proteins to proteomes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4015695/
https://www.ncbi.nlm.nih.gov/pubmed/24593906
http://dx.doi.org/10.1186/1559-0275-11-8
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