Protein O-Galnac Glycosylation: Most Complex and Differentially Regulated PTM

Hiren J. Joshi*, Catharina Steentoft, Katrine T.B.G. Schjoldager, Sergey Y. Vakhrushev, Hans H. Wandall, Henrik Clausen

*Corresponding author for this work
3 Citations (Scopus)

Abstract

Recent advances in O-glycoproteomics strategies have resulted in substantial progress in identification and characterization of O-glycoproteins, and this is particularly true for the mucin-type or GalNAc-type O-glycosylation. Highthroughput mass spectrometric methods have produced large quantities of O-glycosite data, allowing us to finally produce more comprehensive maps of sites of O-glycosylation. In this chapter we discuss this explosion of data, the implication it has upon our understanding of the nature of GalNAc-type O-glycosylation, and the development of bioinformatic tools to aid our comprehension of the O-glycoproteome. As tools to aid comprehension, predictors of O-glycosylation such as NetOGlyc4.0 allow us to make estimates about the nature of the complete O-glycoproteome, while tools such as the Glyco Domain Viewer help us focus on individual proteins and better understand the protein context of the glycosites. We explore some of the concepts that surround these bioinformatics tools and provide some perspective as to how these tools can be further developed to support the study of glycosylation in biology and medicine.

Original languageEnglish
Title of host publicationGlycoscience : Biology and Medicine
Number of pages16
PublisherSpringer Japan
Publication date1 Jan 2015
Pages1049-1064
ISBN (Print)9784431548409
ISBN (Electronic)9784431548416
DOIs
Publication statusPublished - 1 Jan 2015

Keywords

  • Bioinformatics
  • GALNT
  • ISOGlyP
  • NetOGlyc4.0
  • Simple Cell

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