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首页> 外文期刊>Genes to cells : >NEK6-mediated phosphorylation of human TPP1 regulates telomere length through telomerase recruitment
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NEK6-mediated phosphorylation of human TPP1 regulates telomere length through telomerase recruitment

机译：NEK6介导的人类TPP1磷酸化通过端粒酶募集来调节端粒长度

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摘要

Shelterin component TPP1 plays critical roles in chromosome end protection and telomere length regulation. Specifically, TPP1 contains an OB-fold domain that provides an interface to recruit telomerase. However, it remains largely unknown how telomerase recruitment is regulated by cell cycle regulators. We show that TPP1 interacts with the cell cycle regulator kinase NEK6 in human cells. We found that NEK6-mediated phosphorylation of TPP1 Ser255 in G2/M phase regulates the association between telomerase activity and TPP1. Furthermore, we found evidence that POT1 negatively regulates TPP1 phosphorylation because the level of Ser255 phosphorylation was elevated when telomeres were elongated by a POT1 mutant lacking its OB-fold domains. Ser255 is located in the intervening region between the telomerase-recruiting OB-fold and the POT1 recruitment domains. Ser255 and the surrounding amino acids are conserved among vertebrates. These observations suggest that a region adjacent to the OB-fold domain of TPP1 is involved in telomere length regulation via telomerase recruitment.
机译：Shelterin组分TPP1在染色体末端保护和端粒长度调节中起关键作用。具体地说，TPP1包含一个OB折叠域，该域提供了募集端粒酶的接口。然而，在很大程度上尚不清楚细胞周期调节剂如何调节端粒酶募集。我们显示TPP1与人类细胞中的细胞周期调节激酶NEK6相互作用。我们发现，NEK6介导的G2 / M期TPP1 Ser255的磷酸化调节端粒酶活性与TPP1之间的关联。此外，我们发现有证据表明POT1负调节TPP1磷酸化，因为当端粒被缺乏OB折叠域的POT1突变体延长时，Ser255磷酸化水平升高。 Ser255位于端粒酶募集的OB折叠和POT1募集域之间的中间区域。 Ser255和周围的氨基酸在脊椎动物中是保守的。这些观察结果表明，邻近TPP1 OB折叠结构域的区域通过端粒酶募集参与端粒长度调节。

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