Detection and analysis of (O-linked β-N-acetylglucosamine)-modified proteins

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked β-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.

Original languageEnglish (US)
Title of host publicationThe Nucleus
Subtitle of host publicationVolume 2: Chromatin, Transcription, Envelope, Proteins, Dynamics, and Imaging
Pages227-254
Number of pages28
DOIs
StatePublished - 2008

Publication series

NameMethods in Molecular Biology
Volume464
ISSN (Print)1064-3745

Keywords

  • Affinity purification
  • Glycomics
  • Mass spectrometry
  • O-GlcNAc
  • Posttranslational modification
  • Protein glycosylation
  • Signal transduction
  • Site-mapping

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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