朊蛋白前体（PrPC）通过含有α-螺旋1的牛PrP154 - 182与四跨膜蛋白-7相互作用。
PrPC interacts with tetraspanin-7 through bovine PrP154-182 containing alpha-helix 1.
作者信息
Guo Mingxiong, Huang Tao, Cui Yejian, Pan Baiqun, Shen Ao, Sun Yuting, Yi Yourong, Wang Yan, Xiao Gengfu, Sun Guihong
机构信息
The State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.
出版信息
Biochem Biophys Res Commun. 2008 Jan 4;365(1):154-7. doi: 10.1016/j.bbrc.2007.10.160. Epub 2007 Nov 5.
The cellular prion protein (PrP(C)) is highly conserved in the evolution of mammals, and therefore, thought to have important cellular functions. Despite decades of intensive research, the physiological function of PrP(C) remains enigmatic. We carried out a yeast two-hybrid screen on a bovine brain cDNA expression library and identified the transmembrane protein tetraspanin-7 (CD231), as a PrP(C) interacting protein. We confirmed the interaction between PrP(C) and tetraspanin-7 by yeast two-hybrid assay, immunofluorescent co-localization, and immunocoprecipitation. Our mutational studies further demonstrated that PrP(C) specifically binds tetraspanin-7 through the region corresponding to bovine PrP(154-182) containing alpha-helix 1.
细胞朊蛋白（PrP(C)）在哺乳动物进化过程中高度保守，因此被认为具有重要的细胞功能。尽管经过数十年的深入研究，PrP(C)的生理功能仍然成谜。我们对牛脑cDNA表达文库进行了酵母双杂交筛选，并鉴定出跨膜蛋白四跨膜蛋白-7（CD231）为PrP(C)相互作用蛋白。我们通过酵母双杂交分析、免疫荧光共定位和免疫共沉淀证实了PrP(C)与四跨膜蛋白-7之间的相互作用。我们的突变研究进一步表明，PrP(C)通过与包含α-螺旋1的牛PrP(154 - 182)相对应的区域特异性结合四跨膜蛋白-7。
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