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

Title
O-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells
Authors
Song, MKim, HSParka, JMKim, SHKim, IHRyu, SHSuh, PG
POSTECH Authors
Ryu, SH
Date Issued
Jan-2008
Publisher
ELSEVIER SCIENCE INC
Abstract
Post-translational modification of cellular proteins by beta-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. (C) 2007 Elsevier Inc. All rights reserved.
Keywords
o-GlcNAc transferase; Ca2+/calmodulin-dependent kinase IV; depolarization; tissue inhibitor of metalloproteinases-1; AP-1; LINKED N-ACETYLGLUCOSAMINE; PROTEIN MODIFICATION; NUCLEOCYTOPLASMIC PROTEINS; TETRATRICOPEPTIDE REPEATS; SUBSTRATE-SPECIFICITY; CYTOSOLIC PROTEINS; TISSUE INHIBITOR; KINASE-II; GLYCOSYLATION; NUCLEAR
URI
http://oasis.postech.ac.kr/handle/2014.oak/22985
DOI
10.1016/J.CELLSIG.20
ISSN
0898-6568
Article Type
Article
Citation
CELLULAR SIGNALLING, vol. 20, no. 1, page. 94 - 104, 2008-01
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 RYU, SUNG HO
Dept of Life Sciences
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