Site-specific interplay between O-GlcNAcylation and phosphorylation in cellular regulation

Ping Hu, Shino Shimoji, Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

Ser(Thr)-O-linked β-N-acetylglucosamine (O-GlcNAc) is a ubiquitous modification of nucleocytoplasmic proteins. Extensive crosstalk exists between O-GlcNAcylation and phosphorylation, which regulates signaling in response to nutrients/stress. The development of novel O-GlcNAc detection and enrichment methods has improved our understanding of O-GlcNAc functions. Mass spectrometry has revealed O-GlcNAc's many interactions with phosphorylation-mediated signaling. However, mechanisms regulating O-GlcNAcylation and phosphorylation are quite different. Phosphorylation is catalyzed by hundreds of distinct kinases. In contrast, in mammals, uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyl transferase (OGT) and β-D-N-acetylglucosaminidase (OGA) are encoded by single highly conserved genes. Both OGT's and OGA's specificities are determined by their transient associations with many other proteins to create a multitude of specific holoenzymes. The extensive crosstalk between O-GlcNAcylation and phosphorylation represents a new paradigm for cellular signaling.

Original languageEnglish (US)
Pages (from-to)2526-2538
Number of pages13
JournalFEBS Letters
Volume584
Issue number12
DOIs
StatePublished - Jun 2010

Keywords

  • Mass spectrometry
  • O-GlcNAc
  • O-GlcNAcylation
  • OGA
  • OGT
  • Phosphorylation
  • Signaling

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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