A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development

Daniel Mariappa, Nithya Selvan, Vladimir S. Borodkin, Jana Alonso , Andrew T. Ferenbach, Claire Shepherd, Iva Hopkins Navratilova, Daan M. F. Van Aalten (Lead / Corresponding author)

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-Nacetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.

Original languageEnglish
Pages (from-to)255-262
Number of pages8
JournalBiochemical Journal
Volume470
Issue number2
DOIs
Publication statusPublished - Sep 2015

Keywords

  • Drosophila
  • Embryonic development
  • Fluorescence polarization
  • O-GlcNAc probe
  • O-GlcNAcase (OGA)

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