Interaction of calcineurin with a domain of the transcription factor NFAT1 that controls nuclear import
Interaction of calcineurin with a domain of the transcription factor NFAT1 that controls nuclear import
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DOI：
10.1073/pnas.93.17.8907
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发表时间：
1996-08-20
影响因子：
11.1
通讯作者：
Rao, A
中科院分区：
文献类型：
--
作者：
Luo, C;Shaw, KTY;Rao, A
活化T细胞核因子（NFAT）家族转录因子的核输入由蛋白磷酸酶钙调磷酸酶启动。在这里，我们确定了一个调节区NFAT 1，N端的DNA结合域，控制核输入的NFAT 1，NFAT 1的调节区直接结合到钙调神经磷酸酶，是一个底物的钙调神经磷酸酶在体外，并显示调节亚细胞定位相同的全长NFAT 1。NFATc的相应区域同样结合钙调磷酸酶，这表明钙调磷酸酶对NFAT1和NFATc的有效激活反映了磷酸酶对这些蛋白质的特异性靶向。在其他NFAT家族转录因子中存在来自NFAT1调控区的几个序列基序，包括其可能的核定位序列，表明保守的蛋白质结构域可以控制所有NFAT蛋白质的核输入。
The nuclear import of the nuclear factor of activated T cells (NFAT)-family transcription factors is initiated by the protein phosphatase calcineurin. Here we identify a regulatory region of NFAT1, N terminal to the DNA-binding domain, that controls nuclear import of NFAT1, The regulatory region of NFAT1 binds directly to calcineurin, is a substrate for calcineurin in vitro, and shows regulated subcellular localization identical to that of full-length NFAT1. The corresponding region of NFATc likewise binds calcineurin, suggesting that the efficient activation of NFAT1 and NFATc by calcineurin reflects a specific targeting of the phosphatase to these proteins, The presence in other NFAT-family transcription factors of several sequence motifs from the regulatory region of NFAT1, including its probable nuclear localization sequence, indicates that a conserved protein domain may control nuclear import of all NFAT proteins.