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The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy

机译:COP1 E3连接酶与FIP200相互作用,FIP200是哺乳动物自噬的关键调节因子

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The ubiquitin ligase COP1, COnstitutively Photomorphogenic 1, functions in many biological responses in mammalian cells, but its downstream pathway remains unclear. Here, we identified FIP200, a key regulator of mammalian autophagy, as a novel COP1-interacting protein by yeast two-hybrid screening. The interaction was confirmed by a GST-pulldown assay. Split-GFP analysis revealed that interaction between COP1 and FIP200 predominantly occurred in the cytoplasm and was enhanced in cells treated with UV irradiation. Different forms of FIP200 protein were expressed in cultured mammalian cells, and ectopic expression of COP1 reduced one of such forms. These data suggest that COP1 modulates FIP200-associated activities, which may contribute to a variety of cellular functions that COP1 is involved in.
机译:泛素连接酶COP1,组成型为光形态发生蛋白1,在哺乳动物细胞的许多生物学反应中起作用,但其下游途径仍不清楚。在这里,我们通过酵母双杂交筛选确定了哺乳动物自噬的关键调控因子FIP200作为一种新型的COP1相互作用蛋白。通过GST-下拉测定法证实了相互作用。 Split-GFP分析显示,COP1和FIP200之间的相互作用主要发生在细胞质中,并在用UV辐射处理的细胞中增强。在培养的哺乳动物细胞中表达了不同形式的FIP200蛋白,COP1的异位表达减少了其中一种形式。这些数据表明COP1调节FIP200相关的活动,这可能有助于COP1参与多种细胞功能。

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