Intracellular glycosylation and development.
O-linked N-acetylglucosamine (O-GlcNAc) is a highly dynamic post-translational modification of cytoplasmic and nuclear proteins. Although the function of this abundant modification is yet to be definitively elucidated, all O-GlcNAc proteins are phosphoproteins. Further, the serine and threonine residues substituted with O-GlcNAc are often sites of, or close to sites of, protein phosphorylation. This implies that there may be a dynamic interplay between these two post-translational modifications to regulate protein function. In this review, the functions of some of the proteins that are modified by O-GlcNAc will be considered in the context of the potential role of the O-GlcNAc modification. Furthermore, predictions will be made as to how cellular function and developmental regulation might be affected by changes in O-GlcNAc levels.
O'Donnell
Niall
N
Department of Cellular and Molecular Medicine, The Howard Hughes Medical Institute, Glycobiology Research and Training Center, University of California San Diego, La Jolla 92093, USA.
D000818:Animals; D005314:Embryonic and Fetal Development; D006031:Glycosylation; D006801:Humans; D007424:Intracellular Fluid; D051379:Mice; D017351:N-Acetylglucosaminyltransferases / Q000235:genetics / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000096:biosynthesis / Q000378:metabolism*
D011506:Proteins; D014537:Uridine Diphosphate N-Acetylglucosamine; D017351:N-Acetylglucosaminyltransferases