MS-based proteomics for comprehensive investigation of protein O-GlcNAcylation

被引：7

作者：

Xu, Senhan ^{[1
,2
]}

Sun, Fangxu ^{[1
,2
]}

Tong, Ming ^{[1
,2
]}

Wu, Ronghu ^{[1
,2
]}

机构：

[1] Georgia Inst Technol, Sch Chem & Biochem, Atlanta, GA 30332 USA

[2] Georgia Inst Technol, Petit Inst Bioengn & Biosci, Atlanta, GA 30332 USA

来源：

MOLECULAR OMICS | 2021年 / 17卷 / 02期

基金：

美国国家科学基金会;

关键词：

GLCNAC-MODIFIED PROTEINS; HEXOSAMINE BIOSYNTHETIC-PATHWAY; DISSOCIATION MASS-SPECTROMETRY; METABOLIC CHEMICAL REPORTER; LINKED N-ACETYLGLUCOSAMINE; SITE-SPECIFIC ANALYSIS; CELL-SURFACE; CLICK CHEMISTRY; ENRICHMENT METHOD; IDENTIFICATION;

D O I：

10.1039/d1mo00025j

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein O-GlcNAcylation refers to the covalent binding of a single N-acetylglucosamine (GlcNAc) to the serine or threonine residue. This modification primarily occurs on proteins in the nucleus and the cytosol, and plays critical roles in many cellular events, including regulation of gene expression and signal transduction. Aberrant protein O-GlcNAcylation is directly related to human diseases such as cancers, diabetes and neurodegenerative diseases. In the past decades, considerable progress has been made for global and site-specific analysis of O-GlcNAcylation in complex biological samples using mass spectrometry (MS)-based proteomics. In this review, we summarized previous efforts on comprehensive investigation of protein O-GlcNAcylation by MS. Specifically, the review is focused on methods for enriching and site-specifically mapping O-GlcNAcylated peptides, and applications for quantifying protein O-GlcNAcylation in different biological systems. As O-GlcNAcylation is an important protein modification for cell survival, effective methods are essential for advancing our understanding of glycoprotein functions and cellular events.

引用

页码：186 / 196

页数：11

共 106 条

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