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首页> 外文期刊>Cell cycle >Regulation of APC/C(Cdh1) ubiquitin ligase in differentiation of human embryonic stem cells.
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Regulation of APC/C(Cdh1) ubiquitin ligase in differentiation of human embryonic stem cells.

机译：APC / C（Cdh1）泛素连接酶在人类胚胎干细胞分化中的调控。

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摘要

We have recently shown that Skp2 levels are high in undifferentiated human embryonic stem cells, but decline rapidly following induction of differentiation, thereby leading to accumulation of p27. Changes in Skp2 levels were found to be caused mainly by its rate of degradation. Here we show that the activity of APC/C(Cdh1), the ubiquitin ligase that targets Skp2 for degradation, increases markedly during the differentiation process of human embryonic stem cells. APC/C(Cdh1) is present but inactive in undifferentiated embryonic stem cells and becomes active in the differentiated state. The rise in APC/C(Cdh1) activity with differentiation appears to be due, at least in part, to a dramatic decline in the levels of its inhibitor Emi1. In addition, protein kinase activity also appears to contribute to the suppression of APC/C(Cdh1) activity in undifferentiated stem cells, possibly by inhibitory phosphorylation of Cdh1.
机译：我们最近显示，Skp2水平在未分化的人类胚胎干细胞中较高，但在诱导分化后迅速下降，从而导致p27积累。发现Skp2水平的变化主要是由其降解速率引起的。在这里，我们显示了在人类胚胎干细胞分化过程中，针对Skp2降解的泛素连接酶APC / C（Cdh1）的活性显着增加。 APC / C（Cdh1）存在，但在未分化的胚胎干细胞中无活性，并在分化状态下有活性。 APC / C（Cdh1）活性随分化的增加似乎至少部分是由于其抑制剂Emi1的水平急剧下降所致。此外，蛋白激酶活性似乎也可能通过抑制Cdh1磷酸化来抑制未分化干细胞中的APC / C（Cdh1）活性。

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