REFERENCES



Choose an author or browse all
Choose the species or browse all
Choose a criteria for sorting
 Reverse sorting
Search for a protein
Search for a single PMID
Select O-GlcNAc references filter

Click to expand (1 result)


Lefebvre T, Baert F, Bodart JF, Flament S, Michalski JC, Vilain JP. Modulation of O-GlcNAc glycosylation during Xenopus oocyte maturation. Journal of cellular biochemistry 2004 93(5) 15389870
Abstract:
O-linked N-acetylglucosamine (O-GlcNAc) glycosylation is a post-translational modification, which is believed antagonises phosphorylation. We have studied the O-GlcNAc level during Xenopus oocyte meiotic resumption, taking advantage of the high synchrony of this model which is dependent upon a burst of phosphorylation. Stimulation of immature stage VI oocytes using progesterone was followed by a 4.51 +/- 0.32 fold increase in the GlcNAc content, concomitantly to an increase in phosphorylation, notably on two cytoplasmic proteins of 66 and 97 kDa. The increase of O-GlcNAc for the 97 kDa protein, which we identified as beta-catenin was partly related to its accumulation during maturation, as was demonstrated by the use of the protein synthesis inhibitor--cycloheximide. Microinjection of free GlcNAc, which inhibits O-glycosylated proteins-lectins interactions, delayed the progesterone-induced maturation without affecting the O-GlcNAc content. Our results suggest that O-GlcNAc glycosylation could regulate protein-protein interactions required for the cell cycle kinetic.
O-GlcNAc proteins:
CTNB1
Species: Xenopus laevis
Download
Page 1 of 1