Unit

UNIT 24.10 Analysis of Protein O-GlcNAcylation by Mass Spectrometry

  1. Junfeng Ma,
  2. Gerald W. Hart

Published Online: 2 FEB 2017

DOI: 10.1002/cpps.24

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Ma, J., and Hart, G.W. 2017. Analysis of protein O-GlcNAcylation by Mass Spectrometry. Curr. Protoc. Protein Sci. 87:24.10.1-24.10.16. doi: 10.1002/cpps.24

Author Information

  1. Department of Biological Chemistry, The Johns Hopkins University, School of Medicine, Baltimore, Maryland

Publication History

  1. Published Online: 2 FEB 2017

Abstract

O-linked β-d-N-acetyl glucosamine (O-GlcNAc) addition (O-GlcNAcylation), a post-translational modification of serine/threonine residues of proteins, is involved in diverse cellular metabolic and signaling pathways. Aberrant O-GlcNAcylation underlies the initiation and progression of multiple chronic diseases including diabetes, cancer, and neurodegenerative diseases. Numerous methods have been developed for the analysis of protein O-GlcNAcylation, but instead of discussing the classical biochemical techniques, this unit covers O-GlcNAc characterization by combining several enrichment methods and mass spectrometry detection techniques [including collision-induced dissociation (CID), higher energy collision dissociation (HCD), and electron transfer dissociation (ETD) mass spectrometry]. © 2017 by John Wiley & Sons, Inc.

Keywords:

  • BEMAD;
  • CID;
  • enrichment;
  • ETD;
  • HCD;
  • mass spectrometry;
  • O-GlcNAc;
  • O-GlcNAcome;
  • O-GlcNAcomics;
  • site mapping