Protein O-GlcNAcylation in diabetes and diabetic complications

Junfeng M.a., Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

127 Scopus citations


The post-translational modification of serine and threonine residues of proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is highly ubiquitous, dynamic and inducible. Protein O-GlcNAcylation serves as a key regulator of critical biological processes including transcription, translation, proteasomal degradation, signal transduction and apoptosis. Increased O-GlcNAcylation is directly linked to insulin resistance and to hyperglycemia-induced glucose toxicity, two hallmarks of diabetes and diabetic complications. In this review, we briefly summarize what is known about protein O-GlcNAcylation and nutrient metabolism, as well as discuss the commonly used tools to probe changes of O-GlcNAcylation in cultured cells and in animal models. We then focus on some key proteins modified by O-GlcNAc, which play crucial roles in the etiology and progression of diabetes and diabetic complications. Proteomic approaches are also highlighted to provide a system view of protein O-GlcNAcylation. Finally, we discuss how aberrant O-GlcNAcylation on certain proteins may be exploited to develop methods for the early diagnosis of pre-diabetes and/or diabetes.

Original languageEnglish (US)
Pages (from-to)365-380
Number of pages16
JournalExpert Review of Proteomics
Issue number4
StatePublished - Aug 2013


  • diabetes
  • diabetic complications
  • hyperglycemia
  • insulin resistance
  • O-GlcNAc
  • O-GlcNAcomics
  • proteomics

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry


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