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首页> 外文期刊>Journal of cellular biochemistry. >Influence of S100A6 on CacyBP/SIP Phosphorylation and Elk-1 Transcriptional Activity in Neuroblastoma NB2a Cells
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Influence of S100A6 on CacyBP/SIP Phosphorylation and Elk-1 Transcriptional Activity in Neuroblastoma NB2a Cells

机译：S100A6对神经母细胞瘤NB2a细胞CacyBP / SIP磷酸化和Elk-1转录活性的影响

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摘要

In this work, we have found that casein kinase II ( CKII) phosphorylates the CacyBP/SIP protein under in vitro conditions and have mapped the phosphorylation site to threonine 184. Moreover, we present evidence that S100A6, a CacyBP/SIP interacting protein, inhibits this phosphorylation in the presence of Ca2+. CacyBP/SIP phosphorylation by CKII was also observed in neuroblastoma NB2a cells. Interestingly, we have found that the effect of DRB, a CKII inhibitor, on CacyBP/SIP phosphorylation state is similar to that of S100A6 overexpression. Phosphorylation at threonine 184 seems to have an effect on CacyBP/SIP phosphatase activity since the T184E phosphorylation mimic mutant overexpressed in NB2a cells has lower phosphatase activity toward p-ERK1/2 when compared to the non-phosphorylable T184A mutant or to the wild-type protein. In conclusion, our data suggest that S100A6 and Ca2+, through inhibiting CacyBP/SIP phosphorylation on threonine 184, are important regulators of CacyBP/SIP phosphatase activity and of ERK1/2-Elk-1 signaling pathway. (C) 2015 Wiley Periodicals, Inc.
机译：在这项工作中，我们发现酪蛋白激酶II（CKII）在体外条件下使CacyBP / SIP蛋白磷酸化，并将磷酸化位点定位在苏氨酸184上。此外，我们提供了证据表明S100A6是CacyBP / SIP相互作用蛋白，可以抑制在Ca2 +存在下进行这种磷酸化。在成神经细胞瘤NB2a细胞中也观察到了CKII引起的CacyBP / SIP磷酸化。有趣的是，我们发现CKII抑制剂DRB对CacyBP / SIP磷酸化状态的影响类似于S100A6过表达。苏氨酸184的磷酸化似乎对CacyBP / SIP磷酸酶活性有影响，因为与不可磷酸化的T184A突变体或野生型相比，NB2a细胞中过表达的T184E磷酸化模拟突变体对p-ERK1 / 2的磷酸酶活性较低。蛋白。总之，我们的数据表明，S100A6和Ca2 +通过抑制苏氨酸184上的CacyBP / SIP磷酸化，是CacyBP / SIP磷酸酶活性和ERK1 / 2-Elk-1信号通路的重要调节剂。 （C）2015威利期刊公司

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