Nucleocytoplasmic glycosylation, O-linked β-N-acetylglucosamine

N. E. Zachara, W. D. Cheung, G. W. Hart

Research output: Contribution to journalReview article

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-N-acetylglucosaminyltransferase, 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.

Original languageEnglish (US)
Pages (from-to)369-383
Number of pages15
JournalCurrent Organic Chemistry
Volume8
Issue number5
DOIs
StatePublished - Mar 1 2004

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ASJC Scopus subject areas

  • Organic Chemistry

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