Intracellular glycosylation and development

• Published in: BBA - General Subjects Vol. 1573; no. 3; pp. 336 - 345
• Main Author: O'Donnell, Niall
• Format: Book Review Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 19.12.2002
• Subjects: animal physiology; Animals; biosynthesis; Embryonic and Fetal Development; genetics; Glycosylation; Humans; Intracellular Fluid; metabolism; Mice; N-Acetylglucosaminyltransferases; N-Acetylglucosaminyltransferases - genetics; N-Acetylglucosaminyltransferases - metabolism; O-GlcNAc; O-GlcNAc transferase; Protein degradation; Proteins; Proteins - metabolism; Transcription factor; UDP-GlcNAc metabolism; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate N-Acetylglucosamine - biosynthesis; Uridine Diphosphate N-Acetylglucosamine - metabolism; Protein degradation; O-GlcNAc transferase; Transcription factor; UDP-GlcNAc metabolism; O-GlcNAc
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(02)00401-4

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.