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USP7 Cooperates with SCML2 To Regulate the Activity of PRC1

机译：USP7与SCML2合作调节PRC1的活性

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摘要

USP7 is a protein deubiquitinase with an essential role in development. Here, we provide evidence that USP7 regulates the activity of Polycomb repressive complex 1 (PRC1) in coordination with SCML2. There are six versions of PRC1 defined by the association of one of the PCGF homologues (PCGF1 to PCGF6) with the common catalytic subunit RING1B. First, we show that SCML2, a Polycomb group protein that associates with PRC1.2 (containing PCGF2/MEL18) and PRC1.4 (containing PCGF4/BMI1), modulates the localization of USP7 and bridges USP7 with PRC1.4, allowing for the stabilization of BMI1. Chromatin immunoprecipitation (ChIP) experiments demonstrate that USP7 is found at SCML2 and BMI1 target genes. Second, inhibition of USP7 leads to a reduction in the level of ubiquitinated histone H2A (H2Aub), the catalytic product of PRC1 and key for its repressive activity. USP7 regulates the posttranslational status of RING1B and BMI1, a specific component of PRC1.4. Thus, not only does USP7 stabilize PRC1 components, its catalytic activity is also necessary to maintain a functional PRC1, thereby ensuring appropriate levels of repressive H2Aub.
机译：USP7是一种蛋白质去泛素酶，在发育中起着至关重要的作用。在这里，我们提供证据表明USP7与SCML2协同调节Polycomb阻抑复合物1（PRC1）的活性。通过PCGF同源物之一（PCGF1至PCGF6）与公共催化亚基RING1B的关联定义了PRC1的六个版本。首先，我们显示SCML2（一种与PRC1.2（包含PCGF2 / MEL18）和PRC1.4（包含PCGF4 / BMI1）关联的多梳基团蛋白）可调节USP7的定位并将USP7与PRC1.4桥接，从而允许BMI1的稳定化。染色质免疫沉淀（ChIP）实验证明USP7位于SCML2和BMI1目标基因上。其次，USP7的抑制导致泛素化组蛋白H2A（H2Aub）（PRC1的催化产物和其阻遏活性的关键）的水平降低。 USP7调节RING1B和BMI1（PRC1.4的特定组成部分）的翻译后状态。因此，USP7不仅能稳定PRC1的成分，而且其催化活性对于维持功能性PRC1也是必要的，从而确保适当水平的H2Aub抑制性。

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