Nucleocytoplasmic glycosylation, O-linked β-N-acetylglucosamine

Natasha E Zachara, W. D. Cheung, Gerald Warren Hart

Research output: Contribution to journalArticle

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 2004

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Glycosylation
Acetylglucosamine
Peptides
Phosphorylation
Proteins
Uridine Diphosphate
Transcription
Nutrients
Phosphotransferases
Genes
Sensors

ASJC Scopus subject areas

  • Organic Chemistry

Cite this

Nucleocytoplasmic glycosylation, O-linked β-N-acetylglucosamine. / Zachara, Natasha E; Cheung, W. D.; Hart, Gerald Warren.

In: Current Organic Chemistry, Vol. 8, No. 5, 03.2004, p. 369-383.

Research output: Contribution to journalArticle

Zachara, Natasha E ; Cheung, W. D. ; Hart, Gerald Warren. / Nucleocytoplasmic glycosylation, O-linked β-N-acetylglucosamine. In: Current Organic Chemistry. 2004 ; Vol. 8, No. 5. pp. 369-383.
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