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Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

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Science  23 Mar 2001:
Vol. 291, Issue 5512, pp. 2376-2378
DOI: 10.1126/science.1058714

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Abstract

The dynamic glycosylation of serine or threonine residues on nuclear and cytosolic proteins by O-linked β-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. Here we systematically examine the current data implicating O-GlcNAc as a regulatory modification important to signal transduction cascades.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. E-mail: gwhart{at}jhmi.edu

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