O-GlcNAc turns twenty: Functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar

Lance Wells, Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

Abstract

O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic nucleocytoplasmic post-translational modification more analogous to phosphorylation than to classical complex O-glycosylation. A large number of nuclear and cytosolic proteins are modified by O-GlcNAc. Proteins modified by O-GlcNAc include transcription factors, signaling components, and metabolic enzymes. While the modification has been known for almost 20 years, functions for the monosaccharide modification are just now emerging. In this review, we will focus on the cycling enzymes and emerging roles for this post-translational modification in regulating signal transduction and transcription. Finally, we will discuss future directions and the working model of O-GlcNAc serving as a nutrient sensor.

Original languageEnglish (US)
Pages (from-to)154-158
Number of pages5
JournalFEBS Letters
Volume546
Issue number1
DOIs
StatePublished - Jul 3 2003

Keywords

  • Diabetes
  • Glycosylation
  • Insulin signaling
  • Nutrient sensing
  • O-GlcNAc
  • Phosphorylation
  • Post-translational modification
  • Transcription

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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