Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism
Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism
复制标题
DOI：
10.1074/jbc.271.39.23603
复制
发表时间：
1996-09-27
影响因子：
4.8
通讯作者：
Norton, JD
中科院分区：
文献类型：
--
作者：
Deed, RW;Armitage, S;Norton, JD
螺旋-环-螺旋蛋白Id家族的成员在细胞生长、分化和发育的控制中作为DNA结合、E蛋白、螺旋-环-螺旋转录因子的负调节剂起作用。通过使用COS细胞的瞬时转染分析，我们表明，在其E蛋白靶的情况下，Id 3蛋白仅定位于细胞质/核周区域。与E蛋白（E47）共转染导致Id 3蛋白的核转位，这是一个需要功能性Id螺旋-环-螺旋二聚化结构域和E蛋白核定位信号的过程。与E蛋白相关的Id 3显示出延长的半衰期，而E蛋白本身更迅速地被转化。这些观察结果表明，E蛋白，通过核伴侣Id，可以调节其自身的抑制性伴侣的可用细胞池。
Members of the Id family of helix-loop-helix proteins function as negative regulators of DNA binding, E protein, helix-loop-helix transcription factors in the control of cell growth, differentiation, and development. By using transient transfection analysis of COS cells, we show that in the absence of its E protein target, the Id3 protein is localized exclusively to the cytoplasm/perinuclear region. Co-transfection with E protein (E47) results in nuclear translocation of the Id3 protein, a process requiring both a functional Id helix-loop-helix dimerization domain and an E protein nuclear localization signal. Id3 that is associated with E protein displays an extended half-life, while the E protein itself is more rapidly turned over. These observations demonstrate that E protein, by nuclear chaperoning Id, can regulate the available cellular pool of its own inhibitory partner.