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首页> 外文期刊>Molecular and Cellular Biology >Mammalian DET1 Regulates Cul4A Activity and Forms Stable Complexes with E2 Ubiquitin-Conjugating Enzymes
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Mammalian DET1 Regulates Cul4A Activity and Forms Stable Complexes with E2 Ubiquitin-Conjugating Enzymes

机译：哺乳动物DET1调节Cul4A活性，并与E2泛素结合酶形成稳定的复合物。

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DET1 (de-etiolated 1) is an essential negative regulator of plant light responses, and it is a component of the Arabidopsis thaliana CDD complex containing DDB1 and COP10 ubiquitin E2 variant. Human DET1 has recently been isolated as one of the DDB1- and Cul4A-associated factors, along with an array of WD40-containing substrate receptors of the Cul4A-DDB1 ubiquitin ligase. However, DET1 differs from conventional substrate receptors of cullin E3 ligases in both biochemical behavior and activity. Here we report that mammalian DET1 forms stable DDD-E2 complexes, consisting of DDB1, DDA1 (DET1, DDB1 associated 1), and a member of the UBE2E group of canonical ubiquitin-conjugating enzymes. DDD-E2 complexes interact with multiple ubiquitin E3 ligases. We show that the E2 component cannot maintain the ubiquitin thioester linkage once bound to the DDD core, rendering mammalian DDD-E2 equivalent to the Arabidopsis CDD complex. While free UBE2E-3 is active and able to enhance UbcH5/Cul4A activity, the DDD core specifically inhibits Cul4A-dependent polyubiquitin chain assembly in vitro. Overexpression of DET1 inhibits UV-induced CDT1 degradation in cultured cells. These findings demonstrate that the conserved DET1 complex modulates Cul4A functions by a novel mechanism.
机译：DET1（去酯化1）是植物光反应的重要负调节剂，它是含有DDB1和COP10泛素E2变体的拟南芥CDD复合物的组成部分。最近已经分离出人DET1作为DDB1和Cul4A相关因子之一，以及Cul4A-DDB1泛素连接酶的一系列含WD40的底物受体。但是，DET1在生化行为和活性方面都不同于cullin E3连接酶的常规底物受体。在这里，我们报告哺乳动物DET1形成稳定的DDD-E2复合物，由DDB1，DDA1（DET1，DDB1相关1）和规范泛素结合酶UBE2E组的成员组成。 DDD-E2复合物与多种泛素E3连接酶相互作用。我们表明，E2成分一旦结合到DDD核心就无法维持泛素硫酯键，从而使哺乳动物DDD-E2等同于拟南芥 CDD复合体。尽管游离的UBE2E-3具有活性并能够增强UbcH5 / Cul4A活性，但DDD核心在体外特异性抑制Cul4A依赖的多聚泛素链装配。 DET1的过表达抑制了培养细胞中紫外线诱导的CDT1降解。这些发现表明，保守的DET1复合物通过一种新颖的机制调节Cul4A功能。

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