Diverse regulation of protein function by O-GlcNAc: A nuclear and cytoplasmic carbohydrate post-translational modification

Keith Vosseller, Kaoru Sakabe, Lance Wells, Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

N-Acetylglucosamine O-linked to serines and threonines of cytosolic and nuclear proteins (O-GlcNAc) is an abundant reversible post-translational modification found in all higher eukaryotes. Evidence for functional regulation of proteins by this dynamic saccharide is rapidly accumulating. Deletion of the gene encoding the enzyme that attaches O-GlcNAc (OGT) is lethal at the single cell level, indicating the fundamental requirement for this modification. Recent studies demonstrate a role for O-GlcNAcylation in processes as diverse as transcription in the nucleus and signaling in the cytoplasm, suggesting that O-GlcNAc has both protein and site-specific influences on biochemistry and metabolism throughout the cell.

Original languageEnglish (US)
Pages (from-to)851-857
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume6
Issue number6
DOIs
StatePublished - Dec 1 2002

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Post Translational Protein Processing
Carbohydrates
Biochemistry
Gene encoding
Acetylglucosamine
Gene Deletion
Threonine
Transcription
Nuclear Proteins
Eukaryota
Metabolism
Serine
Cytoplasm
Proteins
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Diverse regulation of protein function by O-GlcNAc : A nuclear and cytoplasmic carbohydrate post-translational modification. / Vosseller, Keith; Sakabe, Kaoru; Wells, Lance; Hart, Gerald Warren.

In: Current Opinion in Chemical Biology, Vol. 6, No. 6, 01.12.2002, p. 851-857.

Research output: Contribution to journalArticle

Vosseller, Keith ; Sakabe, Kaoru ; Wells, Lance ; Hart, Gerald Warren. / Diverse regulation of protein function by O-GlcNAc : A nuclear and cytoplasmic carbohydrate post-translational modification. In: Current Opinion in Chemical Biology. 2002 ; Vol. 6, No. 6. pp. 851-857.
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