Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc.

  title={Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc.},
  author={Lance Wells and Keith Vosseller and Gerald W. Hart},
  volume={291 5512},
The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) is abundant in all multicellular eukaryotes. On several proteins, O-GlcNAc and O-phosphate alternatively occupy the same or adjacent sites, leading to the hypothesis that one function of this saccharide is to transiently block phosphorylation. The diversity of proteins modified by O-GlcNAc implies its importance in many basic cellular and disease processes… CONTINUE READING
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