Proteomic analysis of steady-state nuclear hormone receptor coactivator complexes
Proteomic analysis of steady-state nuclear hormone receptor coactivator complexes
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DOI：
10.1210/me.2004-0476
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发表时间：
2005-10-01
影响因子：
--
通讯作者：
Qin, J
中科院分区：
文献类型：
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作者：
Jung, SY;Malovannaya, A;Qin, J
我们报告了我们在分析内源性核受体辅激活因子复合物作为核受体信号传导图谱（Nuclear Receptor Signaling Atlas，CNOSA）（www.NURSA.org）的研究桥接链方面的初步努力。一个蛋白质组学的方法是用来系统地分离各种辅激活因子复合物使用HeLa细胞作为模型细胞系，并确定与质谱的辅激活因子相关的蛋白质。我们已经分离并鉴定了7种共激活因子复合物，包括p160类固醇受体共激活因子家族、cAMP反应元件结合蛋白结合蛋白、p300、激活蛋白-1和雌激素受体的共激活因子以及E6乳头瘤病毒相关蛋白。新发现的辅激活子相关蛋白为了解内源性激素受体辅调节子网络及其调节提供了无偏见的线索和联系。我们希望，这些数据的电子可用性，以一般的科学界将促进新的假设的生成和测试，以进一步了解核受体信号和辅激活因子的功能。
We report our initial efforts in the analysis of endogenous nuclear receptor coactivator complexes as a research bridging strand of the Nuclear Receptor Signaling Atlas (NURSA) (www.NURSA.org). A proteomic approach is used to systematically isolate a variety of coactivator complexes using HeLa cells as a model cell line and to identify the coactivator-associated proteins with mass spectrometry. We have isolated and identified seven coactivator complexes including the p160 steroid receptor coactivator family, cAMP response element binding protein-binding protein, p300, coactivator of activating protein-1 and estrogen receptors, and E6 papillomavirus-associated protein. The newly identified coactivator-associated proteins provide unbiased clues and links for understanding of the endogenous hormone receptor coregulator network and its regulation. We hope that the electronic availability of these data to the general scientific community will facilitate generation and testing of new hypotheses to further our understanding of nuclear receptor signaling and coactivator functions.