o-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells

Minseok Song, Hyeon Soo Kim, Ji Man Park, Sun Hee Kim, In Hoo Kim, Sung Ho Ryu, Pann Ghill Suh

Research output: Contribution to journalArticle

43 Citations (Scopus)

Abstract

Post-translational modification of cellular proteins by β-o-linked N-acetylglucosamine (o-GlcNAc) moieties plays a significant role in signal transduction by modulating protein stability, protein-protein interactions, transactivation processes, and the enzyme activities of target proteins. Though various classes of proteins are known to be regulated by o-GlcNAc modification (o-GlcNAcylation), the mechanism that regulates o-linked GlcNAc transferase (OGT) activity remains unknown. Here, we report that potassium chloride-induced depolarization provokes the activation of OGT and subsequent o-GlcNAcylation of proteins in neuroblastoma NG-108-15 cells. Moreover, such an induction of protein o-GlcNAcylation was abolished by treating cells with either a voltage-gated calcium channel inhibitor or a calcium/calmodulin-dependent protein kinase (CaMK) inhibitor. In addition, CaMKIV was found to specifically phosphorylate and activate OGT in vivo and in vitro, which implies that CaMKIV is required for depolarization-induced activation of OGT. Furthermore, we found that OGT is involved in depolarization-induced and CaMKIV-dependent activation of activator protein-1 (AP-1) and subsequent tissue inhibitor of metalloproteinase-1 (Timp-1) gene expression. Taken together, our findings suggest that CaMKIV activated OGT, and OGT has an essential role on the process of CaMKIV-dependent AP-1 activation under depolarization in neuronal cells.

Original languageEnglish
Pages (from-to)94-104
Number of pages11
JournalCellular Signalling
Volume20
Issue number1
DOIs
Publication statusPublished - 2008 Jan

Keywords

  • AP-1
  • Ca/calmodulin-dependent kinase IV
  • Depolarization
  • Tissue inhibitor of metalloproteinases-1
  • o-GlcNAc transferase

ASJC Scopus subject areas

  • Cell Biology

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