Cracking the O-GlcNAc code in metabolism

Hai Bin Ruan, Jay Prakash Singh, Min Dian Li, Jing Wu, Xiaoyong Yang

Research output: Contribution to journalReview articlepeer-review

118 Scopus citations


Nuclear, cytoplasmic, and mitochondrial proteins are extensively modified by O-linked β-. N-acetylglucosamine (. O-GlcNAc) moieties. This sugar modification regulates fundamental cellular processes in response to diverse nutritional and hormonal cues. The enzymes O-GlcNAc transferase (OGT) and O-linked β-. N-acetylglucosaminase (. O-GlcNAcase) mediate the addition and removal of O-GlcNAc, respectively. Aberrant O-GlcNAcylation has been implicated in a plethora of human diseases, including diabetes, cancer, aging, cardiovascular disease, and neurodegenerative disease. Because metabolic dysregulation is a vital component of these diseases, unraveling the roles of O-GlcNAc in metabolism is of emerging importance. Here, we review the current understanding of the functions of O-GlcNAc in cell signaling and gene transcription involved in metabolism, and focus on its relevance to diabetes, cancer, circadian rhythm, and mitochondrial function.

Original languageEnglish (US)
Pages (from-to)301-309
Number of pages9
JournalTrends in Endocrinology and Metabolism
Issue number6
StatePublished - Jun 2013

Bibliographical note

Funding Information:
This work was supported by the National Institutes of Health (R01 DK089098, P01 DK057751), American Diabetes Association, and Ellison Medical Foundation to X.Y., the Brown-Coxe fellowship to H.R., the China Scholarship Council-Yale World Scholars fellowship to M.L., and the Xi’an Jiaotong University international cooperation grant to J.W.


  • Cancer metabolism
  • Circadian rhythm
  • Hexosamine biosynthesis
  • Insulin resistance
  • Mitochondria
  • O-GlcNAc


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