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首页> 外文期刊>Cellular Signalling >Cot/Tp12 and PKC cooperate in the regulation of the transcriptional activity of NFATc2 through the phosphorylation of its amino-terminal domain
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Cot/Tp12 and PKC cooperate in the regulation of the transcriptional activity of NFATc2 through the phosphorylation of its amino-terminal domain

机译：Cot / Tp12和PKC通过其氨基末端结构域的磷酸化合作调节NFATc2的转录活性

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Nuclear factor of activated T cells (NFAT) plays a prominent role in gene transcription during the immune response. Growing evidence demonstrates the implication of inducible phosphorylation of the transactivation domain (TAD) of NFAT in transcriptional activation of genes. We have analyzed the regulation of NFATc2 activation by Cot/Tpl2 and protein kinase C zeta (PKC zeta) in T cells. Our results show that PKC zeta and Cot/Tpl2 cooperate in regulating the transactivation activity mediated by the amino-terminal domain of NFATc2. Neither Cot/Tpl2 kinase nor PKC zeta-mediated induction of the transactivation activity of NFATc2 was affected by cyclosporin-A treatment, supporting a calcineurin independent route in the signaling pathways mediating NFATc2 activation. Co-precipitation experiments showed physical interaction among Cot/Tpl2, PKC zeta and NFATc2. Analysis of the transactivation activity of deletions in the N-terminal region of NFATc2, suggested the involvement of amino acids 52-64 of NFATc2 in the induction of its transactivating function by PKC zeta. This kinase in vitro phosphorylates NFATc2 and deletion and mutational studies identified Ser53 and Ser56 (of the SPPS motif) as substrates for PKC zeta. Thus, our results suggest that PKC zeta phosphorylation of Ser53 and Ser56 in the N-terminal TAD from NFATc2 potentiates its transactivating function in human T cells. (c) 2007 Elsevier Inc. All rights reserved.
机译：在免疫应答过程中，活化T细胞的核因子（NFAT）在基因转录中起着重要作用。越来越多的证据表明，NFAT的反式激活域（TAD）的诱导型磷酸化与基因的转录激活有关。我们已经分析了由Cot / Tpl2和蛋白激酶C zeta（PKC zeta）在T细胞中对NFATc2激活的调节。我们的结果表明，PKC zeta和Cot / Tpl2协同调节NFATc2氨基末端结构域介导的反式激活活性。 Cot / Tpl2激酶和PKC zeta介导的NFATc2反式激活均不受环孢菌素A处理的影响，在介导NFATc2活化的信号传导途径中支持钙调神经磷酸酶非依赖性途径。共沉淀实验表明Cot / Tpl2，PKC zeta和NFATc2之间存在物理相互作用。 NFATc2 N末端区域中的缺失的反式激活活性的分析表明，NFATc2的氨基酸52-64参与了PKC zeta对其反式激活功能的诱导。该激酶在体外使NFATc2磷酸化，缺失和突变研究确定（SPPS主题的）Ser53和Ser56为PKC zeta的底物。因此，我们的结果表明，来自NFATc2的N末端TAD中Ser53和Ser56的PKC zeta磷酸化增强了其在人类T细胞中的反式激活功能。 （c）2007 Elsevier Inc.保留所有权利。

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