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Modulation of O-GlcNAc glycosylation during Xenopus oocyte maturation

Tony Lefebvre1, Frédéric Baert, Jean-François Bodart

  • 1Unité Mixte de Recherches 8576 du CNRS, Glycobiologie Structurale et Fonctionnelle, IFR 118, USTL, Bâtiment C9, 59655 Villeneuve d'Ascq, France. tony.lefebvre@univ-lille1.fr

Journal of Cellular Biochemistry
|September 25, 2004
PubMed

Insights

O-linked N-acetylglucosamine (O-GlcNAc) glycosylation increases during Xenopus oocyte maturation, coinciding with phosphorylation. This modification appears crucial for cell cycle progression and protein interactions.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Developmental Biology

Background:

  • O-linked N-acetylglucosamine (O-GlcNAc) glycosylation is a dynamic post-translational modification.
  • O-GlcNAc glycosylation is often considered antagonistic to phosphorylation.
  • Xenopus oocyte meiotic resumption is a highly synchronized process dependent on phosphorylation.

Purpose of the Study:

  • To investigate the role and dynamics of O-GlcNAc glycosylation during Xenopus oocyte meiotic resumption.
  • To explore the relationship between O-GlcNAc glycosylation and phosphorylation in this model system.

Main Methods:

  • Progesterone stimulation of immature stage VI Xenopus oocytes.
  • Quantification of O-GlcNAc content and phosphorylation.
  • Identification of O-GlcNAc modified proteins using mass spectrometry (implied).
  • Use of cycloheximide to assess protein synthesis dependence.
  • Microinjection of free GlcNAc to disrupt O-glycosylated protein-lectin interactions.

Main Results:

  • Progesterone stimulation led to a significant increase in O-GlcNAc content (4.51-fold).
  • Increased O-GlcNAc levels were observed concomitantly with increased phosphorylation, particularly on 66 and 97 kDa proteins.
  • The 97 kDa protein was identified as beta-catenin; its O-GlcNAc increase was partly due to accumulation during maturation.
  • Microinjection of free GlcNAc delayed progesterone-induced maturation without altering O-GlcNAc levels.

Conclusions:

  • O-GlcNAc glycosylation levels rise during Xenopus oocyte meiotic resumption.
  • O-GlcNAc modification, potentially on beta-catenin, is involved in regulating protein-protein interactions necessary for cell cycle progression.
  • The findings suggest a regulatory role for O-GlcNAc glycosylation in meiotic resumption, possibly modulating phosphorylation-dependent pathways.

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