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DC Field | Value | Language |
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dc.citation.endPage | 104 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 94 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 20 | - |
dc.contributor.author | Song, Minseok | - |
dc.contributor.author | Kim, Hyeon-Soo | - |
dc.contributor.author | Parka, Ji-Man | - |
dc.contributor.author | Kim, Sun-Hee | - |
dc.contributor.author | Kim, In-Hoo | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T09:06:15Z | - |
dc.date.available | 2023-12-22T09:06:15Z | - |
dc.date.created | 2015-01-12 | - |
dc.date.issued | 2008-01 | - |
dc.description.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. | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.20, no.1, pp.94 - 104 | - |
dc.identifier.doi | 10.1016/j.cellsig.2007.09.002 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.scopusid | 2-s2.0-36349032408 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/10100 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=36349032408 | - |
dc.identifier.wosid | 000252579600010 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.title | O-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | o-GlcNAc transferase | - |
dc.subject.keywordAuthor | Ca2+/calmodulin-dependent kinase IV | - |
dc.subject.keywordAuthor | depolarization | - |
dc.subject.keywordAuthor | tissue inhibitor of metalloproteinases-1 | - |
dc.subject.keywordAuthor | AP-1 | - |
dc.subject.keywordPlus | LINKED N-ACETYLGLUCOSAMINE | - |
dc.subject.keywordPlus | PROTEIN MODIFICATION | - |
dc.subject.keywordPlus | NUCLEOCYTOPLASMIC PROTEINS |
- |
dc.subject.keywordPlus | TETRATRICOPEPTIDE REPEATS | - |
dc.subject.keywordPlus | SUBSTRATE-SPECIFICITY | - |
dc.subject.keywordPlus | CYTOSOLIC PROTEINS |
- |
dc.subject.keywordPlus | TISSUE INHIBITOR | - |
dc.subject.keywordPlus | KINASE-II | - |
dc.subject.keywordPlus | GLYCOSYLATION | - |
dc.subject.keywordPlus | NUCLEAR | - |
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