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Current Organic Chemistry

Editor-in-Chief

ISSN (Print): 1385-2728
ISSN (Online): 1875-5348

Nucleocytoplasmic Glycosylation, O-linked β-N-Acetylglucosamine

Author(s): N. E. Zachara, W. D. Cheung and G. W. Hart

Volume 8 , Issue 5 , 2004

Page: [369 - 383] Pages: 15

DOI: 10.2174/1385272043485873

Price: $65

Abstract

O-linked β-N-acetylglucosmaine (O-GlcNAc) is an essential, ubiquitous, dynamic modification of metazoan nucleocytoplasmic proteins. Unlike prototypical glycosylation, O-GlcNAc is not elongated into more complex structures and it is localized almost exclusively to nuclear and cytoplasmic proteins. O-GlcNAc modifies Ser / Thr residues in peptide motifs either identical or similar to those used by kinases. In some instances, O-GlcNAc and phosphorylation occur at the same site, suggesting that a complex interplay exists between these post-translational modifications. Deletion of the gene that adds O-GlcNAc to the protein backbone, the UDP-GlcNAc: polypeptide O-β-Nacetylglucosaminyltransferase, is lethal at the single cell level underlying the importance of O-GlcNAc. O-GlcNAc is rapidly emerging as a key nutrient sensor regulating signaling, transcription and cellular responses to stress.

Keywords: glycosylation, UDP-GlcNAc, phosphorylation, O-b-Nacetylglucosaminyltransferase


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