Glycomic Approaches to Study GlcNAcylation: Protein Identification, Site-mapping, and Site-specific O -GlcNAc Quantitation

Clinical Proteomics

Zihao Wang¹  Gerald W. Hart¹ 

[1] Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, USADepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, USADepartment of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, USA

关键词: Glycomics;    O-GlcNAc;    GlcNAcylation;    Site-mapping;    Chemoenzymatic tagging;   

DOI  :  10.1007/s12014-008-9008-x

来源: Humana Press Inc

【 摘 要 】

Abstract

Background

O-Linked β-N-acetylglucosamine (O-GlcNAc) is an enzyme-catalyzed posttranslational modification of serine or threonine side chains of nuclear and cytoplasmic proteins. O-GlcNAc is present in all metazoans and in viruses that infect eukaryotic cells. GlcNAcylation is dynamic and has a high cycling rate on many proteins in response to cellular metabolism and various environmental stimuli. The rapid cycling of O-GlcNAc modulates many biological processes, including transcriptional regulation, stress responses, cell cycle regulation, and protein synthesis and turnover.

Rationale

Despite the importance of O-GlcNAc, progress during the past two decades in this field has been slow. One of the major obstacles is the lack of simple and sensitive tools for efficient O-GlcNAc detection and localization. Recently developed O-GlcNAc derivatization and enrichment approaches, together with new techniques in mass spectrometric instrumentation and methods, have provided breakthroughs in O-GlcNAc site localization and site-specific quantitation. In this review, we will discuss how the current techniques are expanding our knowledge about O-GlcNAc proteomics/glycomics and functions.

【 授权许可】

Unknown