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

The COP1 E3-ligase interacts with FIP200, a key regulator of mammalian autophagy.
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DOI:
10.1186/1471-2091-14-1
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发表时间:
2013-01-06
期刊:
影响因子:
--
通讯作者:
Kato JY
Kato JY
中科院分区:
生物4区
文献类型:
--
作者:
Kobayashi S;Yoneda-Kato N;Itahara N;Yoshida A;Kato JY

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泛素连接酶COP 1(Constitutively Photomorphogenic 1)在哺乳动物细胞的许多生物反应中起作用,但其下游途径尚不清楚。在这里,我们确定了FIP 200,哺乳动物自噬的关键调节,作为一种新的COP 1相互作用蛋白的酵母双杂交筛选。通过GST-下拉测定证实了相互作用。Split-GFP分析显示,COP 1和FIP 200之间的相互作用主要发生在细胞质中,并在紫外线照射处理的细胞中增强。不同形式的FIP 200蛋白在培养的哺乳动物细胞中表达,并且COP 1的异位表达减少了其中一种形式。这些数据表明,COP 1调节FIP 200相关的活动,这可能有助于COP 1参与的各种细胞功能。
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.
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