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首页> 外文期刊>Cellular Signalling >O-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells
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O-GlcNAc transferase is activated by CaMKIV-dependent phosphorylation under potassium chloride-induced depolarization in NG-108-15 cells

机译：在NG-108-15细胞中，通过氯化钾诱导的去氧的Camkiv依赖性磷酸化激活O-GlcNAc转移酶

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摘要

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.
机译：通过β-O-连接的N-乙酰葡糖胺（O-GlcNAC）部分对细胞蛋白的后翻透修饰在通过调节蛋白质稳定性，蛋白质 - 蛋白质相互作用，转移过程和靶蛋白的酶活性在信号转导中起着重要作用。尽管已知各种蛋白质被O-GlcNAC改性（O-Glcnacylation）调节（O-Glcnacylation），但调节O-连接的GlcNAc转移酶（OGT）活性的机制仍然未知。在这里，我们报告氯化钾诱导的去极化引起了神经母细胞瘤NG-108-15细胞中蛋白质的OGT和随后的O-Glcnacylation的激活。此外，通过用电压门控钙通道抑制剂或钙/钙调蛋白依赖性蛋白激酶（CAMK）抑制剂处理细胞，废除了这种蛋白质O-GlcNacylation的诱导。此外，发现CAMKIV在体内和体外磷酸化并激活OGT，这意味着CAMKIV需要去极化诱导的OGT活化。此外，我们发现OGT参与了活化剂蛋白-1（AP-1）和随后的金属蛋白酶-1（TIMP-1）基因表达的后续组织抑制剂的去极化诱导和CAMKIV依赖性活化。我们的研究结果表明，Camkiv活化OGT，OGT在神经元细胞去极化下Camkiv依赖性AP-1活化过程中具有重要作用。 （c）2007年elestvier Inc.保留所有权利。

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