4.6 Review

Mass Spectrometry for O-GlcNAcylation

Journal

FRONTIERS IN CHEMISTRY
Volume 9, Issue -, Pages -

Publisher

FRONTIERS MEDIA SA
DOI: 10.3389/fchem.2021.737093

Keywords

mass spectrometry; O-GlcNAcylation; O-GlcNAc; O-GlcNAcylated proteins; quali-quantitative charactering; isotope labeling

Funding

  1. Department of Education of Shaanxi Province [20JC035]
  2. National Natural Science Foundation [31300678, 81803002]
  3. Basic Research Program of Natural Science of Shaanxi Province [2016JQ3018]

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O-GlcNAcylation, a crucial protein modification, plays important roles in various biological processes and aberrant levels are linked to diseases. Utilizing mass spectrometry combined with affinity enrichment can provide insights into the structure-function mechanism of O-GlcNAcylation, aiding in understanding its biological functions.
O-linked beta-N-acetylglucosamine modification (O-GlcNAcylation) at proteins with low-abundance expression level and species diversity, shows important roles in plenty of biological processes. O-GlcNAcylations with abnormal expression levels are associated with many diseases. Systematically profiling of O-GlcNAcylation at qualitative or quantitative level is vital for their function understanding. Recently, the combination of affinity enrichment, metabolic labeling or chemical tagging with mass spectrometry (MS) have made significant contributions to structure-function mechanism elucidating of O-GlcNAcylations in organisms. Herein, this review provides a comprehensive update of MS-based methodologies for quali-quantitative characterization of O-GlcNAcylation.

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