中文摘要：

evolutionarily 保存的房间极性蛋白质 Par3，像支架的 PDZreontaining 蛋白质，在上皮的房间极性的建立和维护起一个关键作用。尽管在在上皮的房间建立房间极性的 Par3 的角色强烈地被探索了，在造血的房间的 Par3 的功能留下逃犯。处理这个问题，我们产生了 Par3 PDZ 领域的 GST 熔化蛋白质。由把 GST-pull-down 途径与液体层析双人脚踏车团 spectrometry 相结合，我们在 Jurkat 房间(一根 T 房间线) 识别了 Par3 的 PDZ 领域的 10 潜在的新奇有约束力的蛋白质。有三蛋白质的 Par3 的相互作用—原子运输蛋白质 importin-α4 和 proteasome 使活跃之物 PA28β 和 PA28γ—被证实在 vitro 绑定试金， co-immunoprecipitation 试金和免疫荧光显微镜学使用。我们的结果有潜力揭开在血房间的房间极性蛋白质 Par3 的新奇功能。

英文摘要：

The evolutionarily conserved cell polarity protein Par3, a scaffold-like PDZ-containing protein, plays a critical role in the establishment and maintenance of epithelial cell polarity. Although the role of Par3 in establishing cell polarity in epithelial cells has been intensively explored, the function of Par3 in hematopoietic cells remains elusive. To address this issue, we generated GST-fusion proteins of Par3 PDZ domains. By combining the GST-pull-down approach with liquid chromatography-tandem mass spectrometry, we identified 10 potential novel binding proteins of PDZ domains of Par3 in Jurkat cells （a T-cell line）. The interaction of Par3 with three proteins--nuclear transport protein importin-α4 and proteasome activators PA28β and PA28γ--was confirmed using in vitro binding assay, co-immunoprecipitation assay and immunofluorescence microscopy. Our results have the potential to uncover novel functions of the cell polarity protein Par3 in blood cells.