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首页> 外文期刊>Molecular and Cellular Biology >Simian Virus 40 Small t Antigen Mediates Conformation-Dependent Transfer of Protein Phosphatase 2A onto the Androgen Receptor
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Simian Virus 40 Small t Antigen Mediates Conformation-Dependent Transfer of Protein Phosphatase 2A onto the Androgen Receptor

机译：猿猴病毒40小吨t抗原介导蛋白磷酸酶2A的构象依赖性转移到雄激素受体上。

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摘要

The tumor antigens simian virus 40 small t antigen (ST) and polyomavirus small and medium T antigens mediate cell transformation in part by binding to the structural A subunit of protein phosphatase 2A (PP2A). The replacement of B subunits by tumor antigens inhibits PP2A activity and prolongs phosphorylation-dependent signaling. Here we show that ST mediates PP2A A/C heterodimer transfer onto the ligand-activated androgen receptor (AR). Transfer by ST is strictly dependent on the agonist-activated conformation of AR, occurs within minutes of the addition of androgen to cells, and can occur in either the cytoplasm or the nucleus. The binding of ST changes the conformation of the A subunit, and ST rapidly dissociates from the complex upon PP2A A/C heterodimer binding to AR. PP2A is transferred onto the carboxyl-terminal half of AR, and the phosphatase activity is directed to five phosphoserines in the amino-terminal activation function region 1, with a corresponding reduction in transactivation. Thus, ST functions as a transfer factor to specify PP2A targeting in the cell and modulates the transcriptional activity of AR.
机译：肿瘤抗原猿猴病毒40小T抗原（ST）和多瘤病毒小T和中T抗原部分地通过结合蛋白磷酸酶2A（PP2A）的结构A亚基来介导细胞转化。肿瘤抗原取代B亚基可抑制PP2A活性并延长磷酸化依赖性信号传导。在这里，我们显示ST介导PP2A A / C异二聚体转移到配体激活的雄激素受体（AR）上。 ST的转移严格取决于AR的激动剂激活构象，发生在向细胞添加雄激素的几分钟之内，并且可以发生在细胞质或细胞核中。 PP的结合会改变A亚基的构象，而PP2A A / C异二聚体与AR结合后，ST会迅速从复合物中解离。 PP2A被转移到AR的羧基末端一半，并且磷酸酶的活性被导向氨基末端激活功能区1中的五个磷酸丝氨酸，相应降低了反式激活。因此，ST充当转移因子以指定细胞中的PP2A靶向并调节AR的转录活性。

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