Portal de Periódicos da CAPES

Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc

2001; American Association for the Advancement of Science; Volume: 291; Issue: 5512 Linguagem: Inglês

10.1126/science.1058714

1095-9203

Lance Wells, Keith Vosseller, Gerald W. Hart,

Galectins and Cancer Biology

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.