Minireview series on the thirtieth anniversary of research on O-GlcNAcylation of nuclear and cytoplasmic proteins: Nutrient regulation of cellular metabolism and physiology by O-GlcNAcylation

Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

The dynamic cycling of N-acetylglucosamine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins serves as a nutrient sensor, both independently and also via its interplay with other post-translational modifications, to regulate signaling, transcription, and cellular physiology. Emerging evidence suggests that dysregulation of this ubiquitous post-translational modification contributes to the etiology of some the most important human chronic diseases.

Original languageEnglish (US)
Pages (from-to)34422-34423
Number of pages2
JournalJournal of Biological Chemistry
Volume289
Issue number50
DOIs
StatePublished - Dec 12 2014

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Acetylglucosamine
Physiology
Anniversaries and Special Events
Threonine
Transcription
Post Translational Protein Processing
Nuclear Proteins
Metabolism
Serine
Nutrients
Food
Sensors
Research
Proteins
Chronic Disease

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

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