O-GlcNAc profiling: from proteins to proteomes

Clinical Proteomics

Gerald W Hart¹  Junfeng Ma¹ 

[1] Department of Biological Chemistry, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205-2185, USA

关键词: Mass spectrometry;    Quantification;    Site mapping;    Enrichment;    Proteomics;    O-GlcNAcomics;    O-GlcNAcome;    O-GlcNAc;   

Others  :  802952
DOI  :  10.1186/1559-0275-11-8

 received in 2013-09-30, accepted in 2014-02-01,  发布年份 2014

【 摘 要 】

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.

【 授权许可】

   
2014 Ma and Hart; licensee BioMed Central Ltd.

【 图 表 】

Figure 1.

Figure 2.

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